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Sandipayan_enzyme inhibition_seminar

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seminar on "enzyme inhibition"

seminar on "enzyme inhibition"

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  • Faded picture background with full-color video overlay(Intermediate)To reproduce the background effects on this slide, do the following:On the Home tab, in the Slides group, click Layout, and then click Blank.On the Insert tab, in the Media group, click Video, and then click Video from File. In the left pane of the Insert Video dialog box, click the drive or library that contains the video. In the right pane of the dialog box, click the video that you want and then click Insert.Under Video Tools, on the Format tab, in the Sizing group, click the arrow to the right of Size to launch the Format Video dialog box.In the Format Video dialog box, select Size from the left pane, under Scale in the right pane clear the Lock Aspect Ratio box.In the Format Video dialog box, select Size from the left pane, under Size and Rotate in the right pane, set the Height to 7.5” and set the Width to 10”.On the Home tab, in the Drawing group, click Arrange,point to Align, and then do the following: Click Align Center.Click Align Middle.Select the video. On the Home tab, in the Clipboard group, click Copy.Also on the Home tab, in the Clipboard group, click the arrow below Paste, and select Paste Special. In the Paste Special dialog box, select Paste, and then under As, select Picture (JPEG).Select the (JPEG) image. On the Home tab, in the Drawing group, click Arrange, point to Align, and then do the following:Click Align Top. Click Align Left.Under Picture Tools, on the Format tab, in the Adjust group, click the arrow under Color, and then under Recolor select Tan, Background color 2 Light (third row, first option from the left). On the Home tab, in the Drawing group, click the arrow below Arrange,and select Send to Back.Select the video. Under Video Tools on the Format tab, in the Size group, click the arrow at the bottom right corner to launch the Format Video dialog box, and then select Crop in the left pane. In the Crop pane, under Crop Position do the following:In the Width box, enter 3.17”. In the Height box, enter 7.5”.Also in the Format Video dialog box, select Glow and Soft Edges in the left pane. Under Soft Edges in the right pane, click the arrow next to Presets and select 25 Point.On the Animations tab, in the Animation group, select Play.Also on the Animations tab, in the Timing group, click the arrow to the right of Start and select With Previous.Select the video. Under Video Tools, on the Playback tab, in the Video Options group, select Loop until Stopped.To reproduce the text effects on this slide, do the following:On the Insert tab, in the Text group, click Text Box, and then on the slide drag to draw your text box.With the text box selected type in desired title text (“Title”).Select the text. On the Home tab, in the Font group, click the arrow at the bottom corner to launch the Font dialog box, then on the Font tab do the following:In the Text Font box, select Calibri from the Font list.In the Font Style box, select Bold.In the Size box, enter 36 pt, and then click OK.Also on the Home tab, in the Paragraph group, select the Center Text icon.Under Drawing Tools, on the Format tab, in the WordArt Styles group, click the arrow at the bottom right corner to launch the Format Text Effects box, and then select Reflection in the left pane and in the Reflection pane click the arrow to the right of Presets and under Reflection Variations select Half Reflection 4 pt Offset (second row, second option from left).Also on the Format tab, in the Size group, click the arrow at the bottom right corner to launch the Format Shape dialog box, select Position in the left pane, and in the Position pane do the following:In the Horizontal box, enter 3.16” from Top Left Corner.In the Vertical box, enter 0.5” from Top Left Corner.On the Insert tab, in the Text group, click Text Box, and then on the slide drag to draw your text box.With the text box selected, type in desired body copy text.Select the text. On the Home tab, in the Font group, select Calibri from the Font list, and then select 28 pt from the FontSize list.Under Drawing Tools, on the Format tab, in the Size group, click the arrow at the bottom right corner to launch the Format Shape dialog box, select Position in the left pane, and in the Position pane do the following:In the Horizontal box, enter 3.6” from Top Left Corner.In the Vertical box, enter 2.25” from Top Left Corner.Close the Format Shape dialog.
  • Animated upward process arrow with colored bullets(Basic)To reproduce the SmartArt effects on this slide, do the following:On the Home tab, in the Slides group, click Layout, and then clickBlank. On the Insert tab, in the Illustrations group, click SmartArt. In the Choose a SmartArt Graphic dialog box, in the left pane, click Process. In the Process pane, click Upward Arrow (eighth row, third option from the left), and then click OK to insert the graphic into the slide.Select the graphic, and then click one of the arrows on the left border. In the Type your text here dialog box, enter text. (Note: To create a bulleted list below each heading, select the heading text box in the Type your text here dialog box, and then under SmartArtTools, on the Design tab, in the CreateGraphic group, click AddBullet. Enter text into the new bullet text box.)On the slide, select the graphic. Under SmartArtTools, on the Design tab, in the SmartArtStyles group, do the following:Click ChangeColors, and then under Colorful click Colorful Range - Accent Colors 3 to 4 (third option from the left).Click More, and then under Best Match for Document click Intense Effect (fifth option from the left).On the Home tab, in the Font group, select Calibri from the Font list, and then select 24 from the Font Size list.Select the text in the first text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickOliveGreen, Accent 3, Darker 25% (fifth row, seventh option from the left).Select the text in the second text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickAqua, Accent 5, Darker 25% (fifth row, ninth option from the left).Select the text in the third text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickPurple, Accent 4, Darker 25% (fifth row, eighth option from the left).To reproduce the animation effects on this slide, do the following:On the Animations tab, in the Advanced Animations group, click Animation Pane.On the slide, select the graphic. On the Animations tab, in the Animation group, click the More arrow at the side of the Effects Gallery, and under Entrance, click Wipe.In the Animation group, click Effect Options and do the following:under Direction, click From Left.Under Sequence, click One by One.In the Timing group, do the following:In the Duration list, click 01.00.In the Start list, click With Previous.In the Animation Pane, click the double arrow under the wipe effect to expand the contents of the list of effects.Also in the Animation Pane, select the second wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the third wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the fourth wipe effect, and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the fifth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the sixth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the seventh wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.To reproduce the background effects on this slide, do the following:Right-click the slide background area, and then click Format Background. In the Format Background dialog box, click Fill in the left pane, select Gradient fill in the Fill pane, and then do the following:In the Type list, select Linear.In the Direction list, click Linear Right (first row, fourth option from the left).Under Gradient stops, click Add gradient stop or Remove gradient stop until two stops appear on the slider, then customize the gradient stops as follows:Select the first stop on the slider, and do the following:In the Position box, enter 39%.Click the button next to Color, and then under Theme Colors click White, Background 1 (first row, first option from the left).Selectthe last stop on the slider, and do the following: In the Position box, enter 100%.Click the button next to Color, and then under Theme Colors click Olive Green, Accent 3, Lighter 60%(third row, seventh option from the left).To increase the size of the SmartArt graphic so that it spans the entire slide, do the following:On the slide, select the graphic. Point to the top right corner of the graphic border, until a two-headed arrow appears. Drag the top right corner of the graphic border into the top right corner of the slide. Point to the bottom left corner of the graphic border, until a two-headed arrow appears. Drag the bottom left corner of the graphic border into the bottom left corner of the slide.
  • Animated upward process arrow with colored bullets(Basic)To reproduce the SmartArt effects on this slide, do the following:On the Home tab, in the Slides group, click Layout, and then clickBlank. On the Insert tab, in the Illustrations group, click SmartArt. In the Choose a SmartArt Graphic dialog box, in the left pane, click Process. In the Process pane, click Upward Arrow (eighth row, third option from the left), and then click OK to insert the graphic into the slide.Select the graphic, and then click one of the arrows on the left border. In the Type your text here dialog box, enter text. (Note: To create a bulleted list below each heading, select the heading text box in the Type your text here dialog box, and then under SmartArtTools, on the Design tab, in the CreateGraphic group, click AddBullet. Enter text into the new bullet text box.)On the slide, select the graphic. Under SmartArtTools, on the Design tab, in the SmartArtStyles group, do the following:Click ChangeColors, and then under Colorful click Colorful Range - Accent Colors 3 to 4 (third option from the left).Click More, and then under Best Match for Document click Intense Effect (fifth option from the left).On the Home tab, in the Font group, select Calibri from the Font list, and then select 24 from the Font Size list.Select the text in the first text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickOliveGreen, Accent 3, Darker 25% (fifth row, seventh option from the left).Select the text in the second text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickAqua, Accent 5, Darker 25% (fifth row, ninth option from the left).Select the text in the third text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickPurple, Accent 4, Darker 25% (fifth row, eighth option from the left).To reproduce the animation effects on this slide, do the following:On the Animations tab, in the Advanced Animations group, click Animation Pane.On the slide, select the graphic. On the Animations tab, in the Animation group, click the More arrow at the side of the Effects Gallery, and under Entrance, click Wipe.In the Animation group, click Effect Options and do the following:under Direction, click From Left.Under Sequence, click One by One.In the Timing group, do the following:In the Duration list, click 01.00.In the Start list, click With Previous.In the Animation Pane, click the double arrow under the wipe effect to expand the contents of the list of effects.Also in the Animation Pane, select the second wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the third wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the fourth wipe effect, and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the fifth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the sixth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the seventh wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.To reproduce the background effects on this slide, do the following:Right-click the slide background area, and then click Format Background. In the Format Background dialog box, click Fill in the left pane, select Gradient fill in the Fill pane, and then do the following:In the Type list, select Linear.In the Direction list, click Linear Right (first row, fourth option from the left).Under Gradient stops, click Add gradient stop or Remove gradient stop until two stops appear on the slider, then customize the gradient stops as follows:Select the first stop on the slider, and do the following:In the Position box, enter 39%.Click the button next to Color, and then under Theme Colors click White, Background 1 (first row, first option from the left).Selectthe last stop on the slider, and do the following: In the Position box, enter 100%.Click the button next to Color, and then under Theme Colors click Olive Green, Accent 3, Lighter 60%(third row, seventh option from the left).To increase the size of the SmartArt graphic so that it spans the entire slide, do the following:On the slide, select the graphic. Point to the top right corner of the graphic border, until a two-headed arrow appears. Drag the top right corner of the graphic border into the top right corner of the slide. Point to the bottom left corner of the graphic border, until a two-headed arrow appears. Drag the bottom left corner of the graphic border into the bottom left corner of the slide.
  • Animated upward process arrow with colored bullets(Basic)To reproduce the SmartArt effects on this slide, do the following:On the Home tab, in the Slides group, click Layout, and then clickBlank. On the Insert tab, in the Illustrations group, click SmartArt. In the Choose a SmartArt Graphic dialog box, in the left pane, click Process. In the Process pane, click Upward Arrow (eighth row, third option from the left), and then click OK to insert the graphic into the slide.Select the graphic, and then click one of the arrows on the left border. In the Type your text here dialog box, enter text. (Note: To create a bulleted list below each heading, select the heading text box in the Type your text here dialog box, and then under SmartArtTools, on the Design tab, in the CreateGraphic group, click AddBullet. Enter text into the new bullet text box.)On the slide, select the graphic. Under SmartArtTools, on the Design tab, in the SmartArtStyles group, do the following:Click ChangeColors, and then under Colorful click Colorful Range - Accent Colors 3 to 4 (third option from the left).Click More, and then under Best Match for Document click Intense Effect (fifth option from the left).On the Home tab, in the Font group, select Calibri from the Font list, and then select 24 from the Font Size list.Select the text in the first text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickOliveGreen, Accent 3, Darker 25% (fifth row, seventh option from the left).Select the text in the second text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickAqua, Accent 5, Darker 25% (fifth row, ninth option from the left).Select the text in the third text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickPurple, Accent 4, Darker 25% (fifth row, eighth option from the left).To reproduce the animation effects on this slide, do the following:On the Animations tab, in the Advanced Animations group, click Animation Pane.On the slide, select the graphic. On the Animations tab, in the Animation group, click the More arrow at the side of the Effects Gallery, and under Entrance, click Wipe.In the Animation group, click Effect Options and do the following:under Direction, click From Left.Under Sequence, click One by One.In the Timing group, do the following:In the Duration list, click 01.00.In the Start list, click With Previous.In the Animation Pane, click the double arrow under the wipe effect to expand the contents of the list of effects.Also in the Animation Pane, select the second wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the third wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the fourth wipe effect, and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the fifth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the sixth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the seventh wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.To reproduce the background effects on this slide, do the following:Right-click the slide background area, and then click Format Background. In the Format Background dialog box, click Fill in the left pane, select Gradient fill in the Fill pane, and then do the following:In the Type list, select Linear.In the Direction list, click Linear Right (first row, fourth option from the left).Under Gradient stops, click Add gradient stop or Remove gradient stop until two stops appear on the slider, then customize the gradient stops as follows:Select the first stop on the slider, and do the following:In the Position box, enter 39%.Click the button next to Color, and then under Theme Colors click White, Background 1 (first row, first option from the left).Selectthe last stop on the slider, and do the following: In the Position box, enter 100%.Click the button next to Color, and then under Theme Colors click Olive Green, Accent 3, Lighter 60%(third row, seventh option from the left).To increase the size of the SmartArt graphic so that it spans the entire slide, do the following:On the slide, select the graphic. Point to the top right corner of the graphic border, until a two-headed arrow appears. Drag the top right corner of the graphic border into the top right corner of the slide. Point to the bottom left corner of the graphic border, until a two-headed arrow appears. Drag the bottom left corner of the graphic border into the bottom left corner of the slide.
  • Animated upward process arrow with colored bullets(Basic)To reproduce the SmartArt effects on this slide, do the following:On the Home tab, in the Slides group, click Layout, and then clickBlank. On the Insert tab, in the Illustrations group, click SmartArt. In the Choose a SmartArt Graphic dialog box, in the left pane, click Process. In the Process pane, click Upward Arrow (eighth row, third option from the left), and then click OK to insert the graphic into the slide.Select the graphic, and then click one of the arrows on the left border. In the Type your text here dialog box, enter text. (Note: To create a bulleted list below each heading, select the heading text box in the Type your text here dialog box, and then under SmartArtTools, on the Design tab, in the CreateGraphic group, click AddBullet. Enter text into the new bullet text box.)On the slide, select the graphic. Under SmartArtTools, on the Design tab, in the SmartArtStyles group, do the following:Click ChangeColors, and then under Colorful click Colorful Range - Accent Colors 3 to 4 (third option from the left).Click More, and then under Best Match for Document click Intense Effect (fifth option from the left).On the Home tab, in the Font group, select Calibri from the Font list, and then select 24 from the Font Size list.Select the text in the first text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickOliveGreen, Accent 3, Darker 25% (fifth row, seventh option from the left).Select the text in the second text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickAqua, Accent 5, Darker 25% (fifth row, ninth option from the left).Select the text in the third text box from the left. Under SmartArtTools, on the Format tab, in the WordArtStyles group, click the arrow next to TextFill, and then under Theme Colors clickPurple, Accent 4, Darker 25% (fifth row, eighth option from the left).To reproduce the animation effects on this slide, do the following:On the Animations tab, in the Advanced Animations group, click Animation Pane.On the slide, select the graphic. On the Animations tab, in the Animation group, click the More arrow at the side of the Effects Gallery, and under Entrance, click Wipe.In the Animation group, click Effect Options and do the following:under Direction, click From Left.Under Sequence, click One by One.In the Timing group, do the following:In the Duration list, click 01.00.In the Start list, click With Previous.In the Animation Pane, click the double arrow under the wipe effect to expand the contents of the list of effects.Also in the Animation Pane, select the second wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the third wipe effect and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the fourth wipe effect, and then on the Animations tab, do the following:In the Animation group, click More, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the fifth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.Also in the Animation Pane, select the sixth wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Exciting, click Curve Up, and then click OK.In the Timing group,in the Start list, select On Click. In the Timing group,in the Duration list, select 00.50.Also in the Animation Pane, select the seventh wipe effect, and then on the Animations tab, do the following:In the Animation group, click the More arrow on the Effects Gallery, then click More Entrance Effects. In the Change Entrance Effect dialog box, under Moderate, click Peek In, and then click OK.In the Animation group, click Effect Options and under Direction, click From Top.In the Timing group,do the following:In the Start list, select With Previous. In the Timing group,in the Duration list, select 00.50.In the Delay list, enter 00.50.To reproduce the background effects on this slide, do the following:Right-click the slide background area, and then click Format Background. In the Format Background dialog box, click Fill in the left pane, select Gradient fill in the Fill pane, and then do the following:In the Type list, select Linear.In the Direction list, click Linear Right (first row, fourth option from the left).Under Gradient stops, click Add gradient stop or Remove gradient stop until two stops appear on the slider, then customize the gradient stops as follows:Select the first stop on the slider, and do the following:In the Position box, enter 39%.Click the button next to Color, and then under Theme Colors click White, Background 1 (first row, first option from the left).Selectthe last stop on the slider, and do the following: In the Position box, enter 100%.Click the button next to Color, and then under Theme Colors click Olive Green, Accent 3, Lighter 60%(third row, seventh option from the left).To increase the size of the SmartArt graphic so that it spans the entire slide, do the following:On the slide, select the graphic. Point to the top right corner of the graphic border, until a two-headed arrow appears. Drag the top right corner of the graphic border into the top right corner of the slide. Point to the bottom left corner of the graphic border, until a two-headed arrow appears. Drag the bottom left corner of the graphic border into the bottom left corner of the slide.
  • Transcript

    • 1. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 2. Presented by Sandipayan Dutta MSc Biotechnology 2nd Semester Year-2014. Seminar On Enzyme Inhibitors. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 3. What is an Enzyme? Enzymes are specialized proteins that act as catalysts; they speed up chemical reactions by lowering the activation energy required. Enzymes are NOT used up during a reaction. Enzymes are specific to a particular substrate (reactant). All enzymes are proteins with a very specific 3-D shape. A substrate is the molecule that the enzyme acts upon. The 3-D shape of the enzyme fits a substrate molecule like a lock and key – a perfect fit. Are specific for what they will catalyze Are Reusable End in –ase -Sucrase, Lactase, Maltase © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 4. © Copyright. Sandipayan Dutta. 2014. All rights reserved. How do enzymes Work? Enzymes work by weakening bonds which lowers activation energy.
    • 5. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Free Energy Progress of the reaction Reactants Products Free energy of activation Without Enzyme With Enzyme
    • 6. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Induced-Fit Hypothesis Enzymes are flexible molecules and research shows that enzymes will often change the shape of the active site very slightly so that it is an even more precise fit for the substrate. This phenomenon is known as the induced-fit model of enzyme activity. A change in the configuration of an enzyme’s active site (H+ and ionic bonds are involved). Induced by the substrate.
    • 7. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Lock & Key model of enzyme Lock and Key Analogy: lock = enzyme, key = substrate.
    • 8. © Copyright. Sandipayan Dutta. 2014. All rights reserved. No. Classification Biochemical Properties 1 Oxidoreductases Act on many chemical groupings to add or remove hydrogen atoms. oxidases,dehydrogenases,reductases 2 Transferases Transfer functional groups between donor and acceptor molecules. Kinases are specialized transferases that regulate metabolism by transferring phosphate from ATP to other molecules.AST,ALT,hexokinase 3 Hydrolases Add water across a bond, hydrolyzing it.pepsin,trypsin 4 Lyases Add water, ammonia or carbon dioxide across double bonds, or remove these elements to produce double bonds.arginosuccinase,fumarase 5 Isomerases Carry out many kinds of isomerization: L to D isomerizations, mutase reactions (shifts of chemical groups) and others.racemases,epimerase,cis-trans isomerase 6 Ligases Catalyze reactions in which two chemical groups are joined (or ligated) with the use of energy from ATP. All synthetases (synthase)
    • 9. © Copyright. Sandipayan Dutta. 2014. All rights reserved. What Affects Enzyme Activity? Three factors : 1. Environmental Conditions 2. Cofactors and Coenzymes 3. Enzyme Inhibitors
    • 10. © Copyright. Sandipayan Dutta. 2014. All rights reserved. 1. Environmental Conditions 1. Extreme Temperature are the most dangerous - high temps may denature (unfold) the enzyme. 2. pH (most like 6 - 8 pH near neutral) 3. Ionic concentration (salt ions)
    • 11. © Copyright. Sandipayan Dutta. 2014. All rights reserved. 2. Cofactors and Coenzymes Inorganic substances (zinc, iron) and vitamins (respectively) are sometimes need for proper enzymatic activity. Example: Iron must be present in the quaternary structure - hemoglobin in order for it to pick up oxygen.
    • 12. © Copyright. Sandipayan Dutta. 2014. All rights reserved. 3.Enzyme Inhibitors Inhibition – means the prevention or reduction of function. Enzyme inhibitors are molecules that interact in some way with the enzyme to prevent it from working in the normal manner. Since blocking an enzyme's activity can kill a pathogen or correct a metabolic imbalance, many drugs are enzyme inhibitors. They are also used as herbicides and pesticides. Not all molecules that bind to enzymes are inhibitors; enzyme activators bind to enzymes and increase their enzymatic activity.
    • 13. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Why End a Good Thing? Inhibit means stop! If enzyme action is critical to normal health, then why would we want to stop it? Energy Efficiency – It requires energy to build molecules or break them down. Build up of Toxins – Some products are great until their concentration gets too high – then they become toxic to the cell. (Too much of a good thing!)
    • 14. NO MATTER HOW LARGE THE SUBSTRATE CONCENTRATION,REACTION RATE CAN NEVER EXCEED VMAX. Km IS THE SUBSTRATE CONCENTRATION AT WHICH REACTION RATE IS HALF MAXIMAL. Km REFLECTS THE BINDING AFFINITY OF THE ENZYME FOR THE SUBSTRATE; THE HIGHER THE AFFINITY, THE SMALLER IS KM. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 15. Vo = VMAX [S] [S] + KM Vo = VMAX [S] [S] + KM Km IS CALLED MICHAELIS CONSTANT & IT IS INDEPENDENT OF ENZYME CONC. Km IS CONSTANT FOR ENZYME. IT IS EXPRESSED IN moles/L. MICHAELIS-MENTEN EQUATION LINEWEAVER-BURK PLOT OR THE DOUBLE RECIPROCAL PLOT. USEFUL FOR EXPERIMENTAL DETERMINATION OF KM AND VMAX © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 16. Enzyme inhibitors types • Competitive • Uncompetitive • Non-competitive • Mixed • Partial • Substrate • Allosteric • form strong covalent bonds with the enzymes, rendering it inactive. This effect can’t be overcome by increasing the concentration of the substrate. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 17. 1. Reversible E + I E.I Usually from non-covalent interaction with enzyme. 2. Irreversible E + I E.I Usually from covalent bond with enzyme. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Major classes of enzyme inhibitor
    • 18. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Reversible Inhibitors Can bind either to free enzyme or enzyme- substrate complex (usually non-covalently).
    • 19. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Classification of Reversible Inhibitors • Competitive – bind only to free enzyme • Uncompetitive – bind only to enzyme-substrate Complex • Noncompetitive – bind equally well to free enzyme and enzyme-substrate complex • Mixed – binds to both free enzyme and enzyme substrate complex, but with different affinities.
    • 20. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Partial Inhibition : The inhibition is partial, where Linewever-Burk plot would be linear. Substrate Inhibition : Substrate inhibition occurs when a molecule of substrate binds to one site on the enzyme and then another molecule of substrate binds to a separate site on the enzyme to form a dead-end complex. Allosteric inhibitor : binds to the enzyme at a site distinct from the substrate binding site. It is usually reserved for the enzyme, influences conformational changes which may alter the binding characteristics of the enzyme for the substrate or the subsequent reaction characteristics(or both).
    • 21. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Feed back inhibition Feedback inhibition occurs when there is a chain of reactions that must occur in order to achieve a final product. When enough product has been made, some of the surplus product goes back to an enzyme earlier in the chain and inhibits it. When the surplus product is used up by the cell – the product acting as an inhibitor will be consumed and open the pathway again.
    • 22. Competitive Inhibition © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 23. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 24. • Km = [S] when V = (1/2) Vmax • In the presence of a competitive inhibitor, more substrate is required to reach the uninhibited Velocity • But, given high enough [S], the same Vmax can still be reached Why does a competitive inhibitor have these effects ? © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 25. • “When stress is applied to a system at chemical equilibrium, the equilibrium will shift in the direction that tends to relieve or counteract that stress.” • A competitive inhibitor reduces [E]  Equilibrium shifts toward [E] [E] [S] = K’m increases [ES] Why does a competitive inhibitor have these effects? © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 26. The Lineweaver-Burk plot is diagnostic for competitive inhibition Slope = Km,app Vmax 1 Vmax -1 Km,app 1 [S] Increasing [I] 1 v v =1 Vmax Km,app Vmax 1+ [S] 1 © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 27. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Examples of competitive inhibitors 2,3-biphosphoglycerate Inhibits its own formation by inhibiting biphosphoglycerate mutase  Metabolic regulation by product inhibition. Sulphonamides: widely used in medicine to limit bacterial growth Antifreeze: ethylene glycol competes for active site of alcohol dehydrogenase Ethylene glycol is metabolized to oxalic acid, which crystallizes in kidneys and causes renal failure Can be treated by alcohol infusion A new treatment, approved by the FDA in December 1997, uses the alcohol dehydrogenase inhibitor 4-methylpyrazole (trade name = Antizol). Unlike ethanol, 4-methylpyrazole is not a substrate for the enzyme, is therefore not metabolized.
    • 28. Examples of competitive inhibitors • Malonate vs succinate Enzyme: succinate dehydrogenase • Krebs and his colleagues used malonate to investigate the TCA cycle © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 29. DDT Insecticide • Insecticide that effects ATPase activity – ATPase makes ATP from ADP • DDT is a competitive inhibitor that binds with the active site on ATPase, thus stopping the synthesis of ATP in the mitochondria in the body © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 30. Non Competitive Inhibitors © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 31. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 32. • E and E·S are bound equally by the noncompetitive Inhibitor • Amount of uninhibited enzyme is decreased, so V’max is decreased • E vs. E·S equilibrium is not altered, so K’m is Unchanged • Amount of substrate required to reach ½ Vmax is unchanged, so K’m is unchanged Why does a noncompetitive inhibitor have these effects? © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 33. The Lineweaver-Burk plot is diagnostic for noncompetitive inhibition v =1 Vmax,app Km Vmax,app 1 + [S] 1 Slope = Vmax,app Km 1 Vmax,app -1 Km 1 [S] Increasing [I] 1 v © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 34. Examples of noncompetitive inhibitors • Heavy metals like lead, mercury (breaks disulfide bonds), chromium will act as non-competitive inhibitors • Mono-amine oxidase (MAO) inhibitors that are used as anti- depressants: They covalently react with the enzyme in the liver and effectively remove it. – There are many potent drug interactions with MAO inhibitors. One of these is tyramine, a compound that is present in red wine and aged cheeses – MAO inhibitors and tyramine (blocks neurotransmitter reuptake in the brain)  hypertensive crisis – Patients are still subject to hypertension for as long as two weeks after discontinuing the drug © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 35. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 36. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Difference between competitive & non competitive inhibitors
    • 37. Uncompetitive Inhibitors © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 38. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 39. • Only E·S complex is bound by the uncompetitive Inhibitor • Decrease in E·S means less active enzyme, so apparent maximal velocity (V’max) decreases as well • E vs. E·S equilibrium shifts toward E·S [E] [S] = K’m decreases [ES] Why does an uncompetitive inhibitor have these effects? © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 40. The Lineweaver-Burk plot is diagnostic for uncompetitive inhibition v =1 Vmax,app Km,app Vmax,app 1 + [S] 1 = Vmax Km Vmax,app 1 + [S] 1 1 Vmax,app -1 Km,app 1 [S] Increasing [I]1 v Slope = Vmax Km © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 41. Examples of uncompetitive inhibitors • Lithium and the phosphoinositide cycle: an example of uncompetitive inhibition and its pharmacological consequences Nahorski SR, et al Trends Pharmacol Sci. 1991 Aug;12(8):297- 303 – The ability of lithium to exert profound and selective psychopharmacological effects to ameliorate manic-depressive psychosis has been the focus of considerable research effort. – There is increasing evidence that lithium exerts its therapeutic action by interfering with polyphosphoinositide metabolism in brain and prevention of inositol recycling by an uncompetitive inhibition of inositol monophosphatase © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 42. • Many successful pesticides and drugs are tight-binding inhibitors, but these are difficult to design because of the need to deliver and maintain concentrations at least 1000-fold higher than the inhibition constants • A few pesticides are uncompetitive inhibitors, the best-known example being the herbicide N-phosphonomethylglycine, commonly known as glyphosate or Roundup, an uncompetitive inhibitor of 3- phosphoshikimate 1-carboxyvinyltransferase. Examples of uncompetitive inhibitors © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 43. Examples of uncompetitive inhibitors Kamali and Rawlins, Biopharmaceutics & Drug Disposition, 13(6), 403-409 • The effects of probenecid on zidovudine (a potent HIV inhibitor) glucuronidation were investigated, in vitro, using human liver microsomal preparations • The presence of probenecid: – reduced the Vmax for zidovudine glucuronide formation by more than 60 % – reduced Km by 47 % – uncompetitive inhibition © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 44. Enzyme Inhibition (Mechanism) I I S S S I I I II S Competitive Non-competitive Uncompetitive Different site Compete for active siteInhibitor Substrate CartoonGuideEquationandDescription [I] binds to free [E] only, and competes with [S]; increasing [S] overcomes Inhibition by [I]. [I] binds to free [E] or [ES] complex; Increasing [S] can not overcome [I] inhibition. [I] binds to [ES] complex only, increasing [S] favors the inhibition by [I]. E + S→ES→E + P + I ↓ EI ← ↑ E + S→ES→E + P + + I I ↓ ↓ EI+S→EIS ← ↑ ↑ E + S→ES→E + P + I ↓ EIS ← ↑ E I S © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 45. Km Enzyme Inhibition (Plots) I II Competitive Non-competitive Uncompetitive DirectPlotsDoubleReciprocal Vmax Vmax Km Km’ [S], mM vo [S], mM vo I I Km [S], mM Vmax I Km’ Vmax’Vmax’ Vmax unchanged Km increased Vmax decreased Km unchanged Both Vmax & Km decreased I 1/[S]1/Km 1/vo 1/Vmax I Two parallel lines I Intersect at X axis 1/vo 1/Vmax 1/[S]1/Km 1/[S]1/Km 1/Vmax 1/vo Intersect at Y axis = Km’ © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 46. Partial inhibitors • In some situations, the enzyme can still work with the inhibitor bound, but at a reduced rate Activity of the enzyme can not be driven to zero... • To be sure if the compound is a partial inhibitor or not, one should pay attention to experimental conditions • Lineweaver-Burk plot would be linear, BUT secondary plots of intercept or slope vs [I] will not be linear • Dose-response curves (DRC) and Dixon plots are also different for partial inhibitors – At high [I]  there is a residual fractional activity in DRC – Dixon plots are not linear but hyperbolic © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 47. Mixed Inhibition 1. Always possible 2. Not possible with uncompetitive inhibitors 3. Not possible with competitive inhibitors 4. Not possible with competitive or uncompetitive inhibitors A noncompetitive inhibitor is capable of all four reactions, but the classical noncompetitive inhibitor, as opposed to a mixed one, is a special case. With these inhibitors Ks and Ks' are equal to each other, as are Ki and Ki' © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 48. Mixed Inhibition When [E]0<< [I]0: © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 49. allosteric activator substrate cannot bind allosteric inhibitor allosteric binding site vacant; active site can bind substrate active site altered, substrate can bind allosteric binding site vacant enzyme active site active site altered, can’t bind substrate Allosteric activator/inhibitor © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 50. Substrate inhibition © Copyright. Sandipayan Dutta. 2014. All rights reserved. Inhibition of an enzyme activity by a substrate of the reaction catalyzed by that enzyme; often, this type of inhibition occurs at elevated substrate levels in which the substrate is binding to a second, non-active site on the enzyme. At high concentrations, some substrates also inhibit the enzyme activity. Substrate inhibition occurs with about 20% of all known enzymes. It happens when two molecules of substrate can bind to the enzyme, and thus block activity.
    • 51. Irreversible Inhibition In irreversible inhibition, the inhibitor binds to the enzyme irreversibly through formation of a covalent bond with the enzyme , permanently inactivating the enzyme Enzyme S O I © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 52. Irreversible Inhibition - Reaction Mechanism In irreversible inhibition, the inhibitor permanently inactivates the enzyme. The net effect is to remove enzyme from the reaction. Vmax decreases No effect on Km E + S ES E + P EI + I © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 53. The Michaelis-Menten plot for an irreversible inhibitor looks like noncompetitive inhibition Vmax,app < Vmax Km,app = Km . Vmax Vmax2 1 2 1 Vmax,app Km Km,app [Substrate] ReactionRate - Inhibitor + Inhibitor Vmax,app © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 54. Irreversible inhibition is distinguished from noncompetitive inhibition by plotting Vmax vs [E]t Enzyme is inactivated until all of the irreversible inhibitor is used up © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 55. Irreversible inhibitors decrease Vmax,app, but leave the apparent Km unchanged. Irreversible inhibitors differ from other types of inhibitors because they covalently modify the enzyme. This results in the permanent inhibition of the enzyme activity. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 56. Examples of Irreversible Inhibitors • diisopropylphosphofluoridate –prototype for the nerve gas sarin –permanently inactivates serine proteases by forming a covalent bond with the active site serine © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 57. Penicillin is a suicide inhibitor Glycopeptide transpeptidase catalyzes the formation of cross-links between D- amino acids in the cell walls of bacteria. This enzyme also catalyzes the reverse reaction, the hydrolysis of peptide bonds. During the course of hydrolyzing the strained peptide bond in penicillin, the enzyme activates the inhibitor (penicillin), which then covalently modifies an active site serine in the enzyme. In effect, the enzyme “commits suicide” by hydrolyzing the strained peptide bond in penicillin. glycopeptide transpeptidase OHSer O glycopeptide transpeptidase Ser N S CH3 CH3 COO- H H C C O H N C O H H R N S CH3 COO- H H C C O H N C O H Strained peptide bond Penicillin CH3 R © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 58. Suicide inhibitors work by “tricking” the enzyme into activating the inhibitor, which then forms a covalent bond with the enzyme, leading to its permanent inactivation. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 59. Summary-Enzyme Inhibition • Competitive Inhibitor – Binds to substrate binding site – Competes with substrate – The affinity of the substrate appears to be decreased when inhibitor is present (Km,app >Km) • Noncompetitive inhibitor – Binds to allosteric site – Does not compete with the substrate for binding to the enzyme – The maximum velocity appears to be decreased in the presence of the inhibitor (Vmax,app <Vmax) © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 60. • Uncompetitive Inhibitor –Binds to the enzyme only after the substrate has bound –The affinity of the substrate appears to be increased and the maximum velocity appears to be decreased when inhibitor is present (Km,app <Km, Vmax,app <Vmax), • Irreversible Inhibitor –Covalently modifies and permanently inactivates the enzyme © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 61. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Conclusion There are several motivations to study enzyme inhibition: Distinguish among the different potential mechanisms in multisubstrate reactions Relative binding affinity of competitive inhibitors  active site structure research in the absence of 3-D structure info Control mechanisms in biology: balance of protease and their inhibitors in a tissue  help to achieve homeostasis Commercial applications: Insecticides, weed killers Drugs
    • 62. © Copyright. Sandipayan Dutta. 2014. All rights reserved. Since most clinical drug therapy is based on inhibiting the activity of enzymes, analysis of enzyme inhibition kinetics is fundamental to the modern design of pharmaceuticals Well-known examples of such therapy include the use of methotrexate in cancer chemotherapy to semi-selectively inhibit DNA synthesis of malignant cells the use of aspirin to inhibit the synthesis of prostaglandins which are at least partly responsible for the aches and pains of arthritis the use of sulfa drugs to inhibit the folic acid synthesis that is essential for the metabolism and growth of disease-causing bacteria In addition, many poisons (such as cyanide, carbon monoxide and polychlorinated biphenols (PCBs)) produce their life- threatening effects by means of enzyme inhibition .
    • 63. © Copyright. Sandipayan Dutta. 2014. All rights reserved. References BOOKS READ:  Enzymes; Biochemistry, Biotechnology, Clinical chemistry 2nd edition Page 126-150. Trevor Palmer & Philip Bonner East-West press private limited.  LEHNINGER Principles of Biochemistry 5th edition Page 183-233 Michael M.Cox & David L.Nelson W.H.Freeman & company WEBSITES VISITED:  Search on www.google.com  Search on www.youtube.com
    • 64. Acknowledgement I, Sandipayan Dutta, would like to express my heartfelt gratitude towards our respected principal Dr. A . Nagarathna and our Head of the Department Mrs. Asha.K.K . I would like to give special thanks to Mrs. D.R. Jayashree for assigning me the topic for presentation. My family and friends have always been by my side and it falls as my duty to mention them in this event. © Copyright. Sandipayan Dutta. 2014. All rights reserved.
    • 65. © Copyright. Sandipayan Dutta. 2014. All rights reserved.