2 d electrophoresis
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Two-dimensional protein electrophoresis is a form of gel electrophoresis introduced in 1975 by O'Farrell and Klose that allows for the excellent resolution and separation of mixed proteins. It separates proteins based on a series combination of isoelectric focusing by charge and size-based separation. The sample is placed in a pH gradient gel and an electrical potential is applied. Proteins are then detected using chemical stains and analyzed using 2D gel analysis software. It can be used to analyze proteins, separate proteins with excellent resolution, determine amino acid sequences, and separate DNA.
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2 d gel analysis
This document summarizes the analysis of a 2D gel electrophoresis experiment submitted by Prateek Kumar. 2D gel electrophoresis separates proteins based on their isoelectric point and molecular size, allowing thousands of proteins to be analyzed simultaneously. The document describes the major steps in 2D gel analysis, including sample preparation, gel processing and imaging software, spot detection and matching between gels, and statistical analysis to identify protein expression changes related to external variables. Correlation analysis is used to measure how changes in an external variable like age or disease status correspond to increases or decreases in pixel intensity on the 2D gel images.
DiGE....2-D gel electrophoresis
The document discusses 2D gel electrophoresis and the limitations of conventional 2D gels. It introduces Difference Gel Electrophoresis (DIGE), which uses spectrally distinct fluorescent dyes to label protein samples before running multiple samples on the same 2D gel. This allows direct comparison of protein abundance levels between samples and eliminates gel-to-gel variation. The document outlines the experimental design, statistical analysis software, and advantages of DIGE over conventional 2D gels such as increased accuracy, reduced variation, and ability to detect small protein differences.
2 d page
Two-dimensional gel electrophoresis (2-D electrophoresis) is a powerful technique used to separate complex protein mixtures according to their isoelectric point and molecular weight. The first dimension separates proteins by isoelectric focusing according to pH, while the second dimension separates by molecular size using SDS-PAGE. This allows thousands of proteins to be resolved from samples. After electrophoresis, proteins are visualized through staining to compare expression levels between samples. Analysis software can then quantify and identify differentially expressed proteins, aiding in proteomics research.
Proteomics course 2
2D gel electrophoresis separates proteins based on their isoelectric point (pI) in the first dimension and molecular weight in the second dimension. Amino acids can exist as zwitterions and act as both acids and bases, donating or accepting protons. The isoelectric point is calculated using the Henderson-Hasselbalch equation and titration curves, taking into account the pKa values of amino acid side chains. Detection methods for proteins on 2D gels include staining with dyes or radioactive labeling.
2D GEL ELECTROPHORESIS
2-D electrophoresis is a powerful and widely used method for the analysis of complex protein mixtures extracted from cells, tissues, or other biological samples.
Two-dimensional electrophoresis was first introduced by O’Farrell and Klose in 1975
2-DGE is a multi-step separation technique in which proteins are solubilized and separated according to charge (pI) in the first dimension using IEF, followed by size (molecular weight, MW) using SDS-PAGE in the second dimension.
The separated proteins are stained with coomassie or silver stain to produce a two-dimensional protein reference map.
2 d gel electrophresis
Two-dimensional gel electrophoresis (2D-GE) separates proteins based on two properties - isoelectric focusing (IEF) according to isoelectric point (pI) in the first dimension, and SDS-PAGE according to molecular weight in the second dimension. This allows for high resolution separation of complex protein mixtures. Key steps include sample preparation to solubilize and stabilize proteins, IEF to separate by pI, equilibration then SDS-PAGE to separate by size, and visualization techniques like autoradiography or mass spectrometry for analysis.
2d gel electrophorosis
this ppt will give a brief idea about 2D gel electoprosis. as it is a combination of isoelectric focusing and SDS page. it will explain the principle of isoelectric focusing and the SDS page.
how 2D is advantageous over both this elctrophsosis?
Recommended
2 d gel analysis
This document summarizes the analysis of a 2D gel electrophoresis experiment submitted by Prateek Kumar. 2D gel electrophoresis separates proteins based on their isoelectric point and molecular size, allowing thousands of proteins to be analyzed simultaneously. The document describes the major steps in 2D gel analysis, including sample preparation, gel processing and imaging software, spot detection and matching between gels, and statistical analysis to identify protein expression changes related to external variables. Correlation analysis is used to measure how changes in an external variable like age or disease status correspond to increases or decreases in pixel intensity on the 2D gel images.
DiGE....2-D gel electrophoresis
The document discusses 2D gel electrophoresis and the limitations of conventional 2D gels. It introduces Difference Gel Electrophoresis (DIGE), which uses spectrally distinct fluorescent dyes to label protein samples before running multiple samples on the same 2D gel. This allows direct comparison of protein abundance levels between samples and eliminates gel-to-gel variation. The document outlines the experimental design, statistical analysis software, and advantages of DIGE over conventional 2D gels such as increased accuracy, reduced variation, and ability to detect small protein differences.
2 d page
Two-dimensional gel electrophoresis (2-D electrophoresis) is a powerful technique used to separate complex protein mixtures according to their isoelectric point and molecular weight. The first dimension separates proteins by isoelectric focusing according to pH, while the second dimension separates by molecular size using SDS-PAGE. This allows thousands of proteins to be resolved from samples. After electrophoresis, proteins are visualized through staining to compare expression levels between samples. Analysis software can then quantify and identify differentially expressed proteins, aiding in proteomics research.
Proteomics course 2
2D gel electrophoresis separates proteins based on their isoelectric point (pI) in the first dimension and molecular weight in the second dimension. Amino acids can exist as zwitterions and act as both acids and bases, donating or accepting protons. The isoelectric point is calculated using the Henderson-Hasselbalch equation and titration curves, taking into account the pKa values of amino acid side chains. Detection methods for proteins on 2D gels include staining with dyes or radioactive labeling.
2D GEL ELECTROPHORESIS
2-D electrophoresis is a powerful and widely used method for the analysis of complex protein mixtures extracted from cells, tissues, or other biological samples.
Two-dimensional electrophoresis was first introduced by O’Farrell and Klose in 1975
2-DGE is a multi-step separation technique in which proteins are solubilized and separated according to charge (pI) in the first dimension using IEF, followed by size (molecular weight, MW) using SDS-PAGE in the second dimension.
The separated proteins are stained with coomassie or silver stain to produce a two-dimensional protein reference map.
2 d gel electrophresis
Two-dimensional gel electrophoresis (2D-GE) separates proteins based on two properties - isoelectric focusing (IEF) according to isoelectric point (pI) in the first dimension, and SDS-PAGE according to molecular weight in the second dimension. This allows for high resolution separation of complex protein mixtures. Key steps include sample preparation to solubilize and stabilize proteins, IEF to separate by pI, equilibration then SDS-PAGE to separate by size, and visualization techniques like autoradiography or mass spectrometry for analysis.
2d gel electrophorosis
this ppt will give a brief idea about 2D gel electoprosis. as it is a combination of isoelectric focusing and SDS page. it will explain the principle of isoelectric focusing and the SDS page.
how 2D is advantageous over both this elctrophsosis?
Sds-Page
SDS-PAGE is a standard technique used to separate proteins based on their molecular weight. It involves coating proteins with SDS detergent to linearize them, then running them through a polyacrylamide gel with an electric current which causes smaller proteins to migrate faster, allowing separation based on size. The document provides details on the principle, gel preparation, running the electrophoresis, visualizing results with stains like Coomassie blue or silver stain, and applications like determining protein purity or identification.
Koushik page electrophoresis
Electrophoresis is an analytical technique used to separate and characterize proteins, nucleic acids, and other particles based on their size and charge. It works by applying an electric field to move these molecules through a gel such as agarose or polyacrylamide. Different gel types and concentrations allow separation of molecules by size, including SDS-PAGE which uses SDS to denature proteins and separate them by mass. Electrophoresis has applications in molecular biology, medicine, quality control, and forensics.
Two dimensional gel electrophoresis
This document discusses two-dimensional gel electrophoresis (2DGE), a powerful technique for analyzing complex protein mixtures. 2DGE separates proteins in two steps - first by isoelectric focusing to separate proteins by their isoelectric point, followed by SDS-PAGE to separate by molecular weight. This allows thousands of proteins to be separated simultaneously on a single gel based on these two properties. The document provides details on the principles, protocols, and improvements of the 2DGE technique.
Gel electroporosis
The document discusses SDS gel electrophoresis and blotting techniques. It provides an overview of SDS-PAGE, describing how SDS denatures and coats proteins with negative charges. This allows proteins to be separated by size when run on a polyacrylamide gel with an electric current. It also summarizes Southern blotting for detecting DNA, Northern blotting for detecting RNA, and Western blotting for detecting proteins. All involve separating molecules, transferring them to a membrane, and using probes or antibodies to identify specific sequences or proteins. The techniques have applications in research, forensics, medicine and molecular biology.
Sds page
Polyacrylamide gel electrophoresis (PAGE) is a method used to separate macromolecules like proteins or nucleic acids based on their size and charge. It works by applying an electric current to move the charged molecules through a polyacrylamide gel matrix. Smaller molecules move faster through the gel's pores than larger ones. SDS-PAGE specifically uses sodium dodecyl sulfate detergent to denature proteins and impart a uniform negative charge, allowing separation based primarily on size. The document discusses the principles, procedures, applications and different types of PAGE in detail.
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The document discusses different electrophoresis techniques including paper electrophoresis, gel electrophoresis, polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), and non-SDS PAGE. It describes the basic principles, apparatus, procedures, applications and advantages/disadvantages of each technique. Paper electrophoresis is a simple method that uses filter paper as the support medium while gel electrophoresis uses gels like agarose or polyacrylamide as the support medium. SDS-PAGE and PAGE are variations that separate molecules based on their molecular weight or size.
Electrophoresis presentation
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids based on their size and charge. It works by applying an electric current to move these molecules through a medium like a gel or paper. The document discusses different types of electrophoresis like gel electrophoresis, paper electrophoresis, and isolectric focusing. It also explains how various factors like the molecule's charge, size, and shape affect its movement during electrophoresis.
SDS PAGE by kk sahu sir
INTRODUCTION
HISTORY
PRINCIPLE
What is SDS PAGE ?
PROCEDURE
sample preparation
preparing acrylamide gels
electrophoresis
APPLICATION OF SDS PAGE
CONCLUSION
REFERENCE
Gel electrophoresis 2
Mata kuliah tentang elektroforesis gel 2.Cari lebih banyak lagi di: http://muhammadhabibielecture.blogspot.com/2015/02/materi-kuliah-semester-4.html
ISOELECTRIC FOCUSING
Isoelectric focusing is a technique that separates molecules like proteins based on their isoelectric point, which is the pH at which the molecule has no net charge. It was developed in the 1960s and allows for much better resolution than older techniques. The process involves creating an immobilized pH gradient using carrier ampholytes, loading protein samples, and applying an electric field to cause proteins to migrate to the point in the gradient matching their isoelectric point. The separated proteins can then be visualized through staining. Isoelectric focusing is useful for applications like identifying serum proteins and aiding in proteomics research.
Gel Electrophoresis
Gel electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids based on their size and charge. It involves placing the molecules in an agarose, starch or polyacrylamide gel and applying an electric current, causing the molecules to migrate through the gel at different rates. SDS-PAGE is a common type of gel electrophoresis where sodium dodecyl sulfate is used to denature proteins, allowing separation based on molecular weight. The separated molecules can then be visualized by staining techniques to analyze proteins, detect mutations, and more.
PROTEIN ANALYSIS
PROTEIN ANALYSIS
SDS-PAGE (SDS-polyacrylamide gel electrophoresis)
Isoelectric focussing
High-performance liquid chromatography (HPLC)
Thin-layer chromatography (TLC)
Two-dimensional (2-D) gel electrophoresis
Identification of proteins by 2D gel
Protein identification by 2D gels uses a combination of isoelectric focusing (IEF) and SDS-PAGE. In IEF, proteins are separated based on their isoelectric point using an acrylamide gel containing an ampholyte pH gradient established by an electric current. Next, SDS-PAGE further separates the proteins by size. Finally, the proteins are visualized after staining, allowing identification by their position on the 2D gel based on isoelectric point and molecular weight.
Gel electrophorosis final
Gel electrophoresis is a method used to separate biomolecules like DNA, RNA, and proteins based on their size and charge. It works by applying an electric current to move the negatively charged molecules through a gel, with smaller molecules moving faster through the gel pores than larger ones. Common types of gels used include agarose for separating DNA, polyacrylamide for proteins, and starch for some protein analysis. The document provides details on how gel electrophoresis is performed and its applications in fields like forensics, molecular biology, and biochemistry.
Gel electrophoresis
Gel electrophoresis is a technique used to separate biomolecules like proteins, nucleic acids, and other charged molecules. It works by applying an electric field to move these charged molecules through a gel based on their size and charge. There are different types of gels used like agarose, polyacrylamide, and starch depending on the size of molecules to be separated. Samples are loaded into wells in the gel and an electric current is applied causing molecules to migrate through the gel at different rates. The separated biomolecules can then be visualized based on properties like fluorescence or staining to analyze differences in molecular weights and sizes. Gel electrophoresis has many applications in fields like forensics, molecular biology, genetics, and biochemistry
Applied Biochemistry
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids based on their size and charge. It involves applying an electric field to move molecules through a medium like agarose gel or capillary. Shorter/less charged molecules move faster and are separated from longer/more charged molecules. It is used in laboratories and clinical settings to analyze biological samples and diagnose conditions.
2 d gel electrophoresis
This document summarizes a seminar presentation on 2D electrophoresis. 2D electrophoresis is a technique used to separate mixed proteins based on their isoelectric point and mass. It involves two sequential electrophoretic steps: iso-electric focusing to separate proteins by charge, followed by SDS-PAGE to separate by molecular weight. The document describes the principles, methods, applications and references for 2D electrophoresis.
2 d gel electrophoresis
Separation and identification of proteins in a sample by displacement in 2 dimensions oriented at right-angle to one another.
Gel electrophoresis
The document provides information on gel electrophoresis techniques. It discusses different types of gels like agarose, polyacrylamide, and starch that can be used for electrophoresis. Agarose gel is commonly used to separate macromolecules like nucleic acids and proteins due to its large pore size. Polyacrylamide gel is used to separate smaller molecules and provides better resolution than agarose. SDS-PAGE allows separation based on molecular weight by making all proteins negatively charged. The document outlines the procedures for agarose and polyacrylamide gel electrophoresis and their applications in analyzing proteins and nucleic acids.
Electrophoresis
This document discusses various types of electrophoresis techniques. It begins by explaining that electrophoresis involves charged molecules like proteins and nucleic acids migrating in response to an electrical field. It then discusses different gel types like agarose and polyacrylamide gels that are used as supporting matrices. It also covers techniques like SDS-PAGE, isoelectric focusing, two-dimensional gel electrophoresis, and capillary electrophoresis. The document provides details on how each technique separates molecules based on properties like size, charge, and isoelectric point.
2D-PAGE & DIGE
2D-PAGE is a method is used for the separation and identification of proteins in a complex mixture using two separate dimensions that are run perpendicular to one another.
2D-DIGE is an advanced version of classical two-dimensional gel electrophoresis (2D-PAGE).
The protein samples are labeled with fluorescent dyes and then separated by 2D-PAGE.
PFGE
L’électrophorèse en champ pulsé est le résultat de la combinaison d’une digestion par des enzymes de restriction à faible nombre de sites de coupure et d’une électrophorèse adaptée à la grande taille des produits de digestion. Le résultat est un profil de restriction intéressant tout le génome du microorganisme
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SDS-PAGE is a standard technique used to separate proteins based on their molecular weight. It involves coating proteins with SDS detergent to linearize them, then running them through a polyacrylamide gel with an electric current which causes smaller proteins to migrate faster, allowing separation based on size. The document provides details on the principle, gel preparation, running the electrophoresis, visualizing results with stains like Coomassie blue or silver stain, and applications like determining protein purity or identification.
Koushik page electrophoresis
Electrophoresis is an analytical technique used to separate and characterize proteins, nucleic acids, and other particles based on their size and charge. It works by applying an electric field to move these molecules through a gel such as agarose or polyacrylamide. Different gel types and concentrations allow separation of molecules by size, including SDS-PAGE which uses SDS to denature proteins and separate them by mass. Electrophoresis has applications in molecular biology, medicine, quality control, and forensics.
Two dimensional gel electrophoresis
This document discusses two-dimensional gel electrophoresis (2DGE), a powerful technique for analyzing complex protein mixtures. 2DGE separates proteins in two steps - first by isoelectric focusing to separate proteins by their isoelectric point, followed by SDS-PAGE to separate by molecular weight. This allows thousands of proteins to be separated simultaneously on a single gel based on these two properties. The document provides details on the principles, protocols, and improvements of the 2DGE technique.
Gel electroporosis
The document discusses SDS gel electrophoresis and blotting techniques. It provides an overview of SDS-PAGE, describing how SDS denatures and coats proteins with negative charges. This allows proteins to be separated by size when run on a polyacrylamide gel with an electric current. It also summarizes Southern blotting for detecting DNA, Northern blotting for detecting RNA, and Western blotting for detecting proteins. All involve separating molecules, transferring them to a membrane, and using probes or antibodies to identify specific sequences or proteins. The techniques have applications in research, forensics, medicine and molecular biology.
Sds page
Polyacrylamide gel electrophoresis (PAGE) is a method used to separate macromolecules like proteins or nucleic acids based on their size and charge. It works by applying an electric current to move the charged molecules through a polyacrylamide gel matrix. Smaller molecules move faster through the gel's pores than larger ones. SDS-PAGE specifically uses sodium dodecyl sulfate detergent to denature proteins and impart a uniform negative charge, allowing separation based primarily on size. The document discusses the principles, procedures, applications and different types of PAGE in detail.
Electrophoresis-PAPER ELECTROPHORESIS,GEL ELCTROPHORESIS, PAGE-SDS AND NON-SDS
The document discusses different electrophoresis techniques including paper electrophoresis, gel electrophoresis, polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), and non-SDS PAGE. It describes the basic principles, apparatus, procedures, applications and advantages/disadvantages of each technique. Paper electrophoresis is a simple method that uses filter paper as the support medium while gel electrophoresis uses gels like agarose or polyacrylamide as the support medium. SDS-PAGE and PAGE are variations that separate molecules based on their molecular weight or size.
Electrophoresis presentation
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids based on their size and charge. It works by applying an electric current to move these molecules through a medium like a gel or paper. The document discusses different types of electrophoresis like gel electrophoresis, paper electrophoresis, and isolectric focusing. It also explains how various factors like the molecule's charge, size, and shape affect its movement during electrophoresis.
SDS PAGE by kk sahu sir
INTRODUCTION
HISTORY
PRINCIPLE
What is SDS PAGE ?
PROCEDURE
sample preparation
preparing acrylamide gels
electrophoresis
APPLICATION OF SDS PAGE
CONCLUSION
REFERENCE
Gel electrophoresis 2
Mata kuliah tentang elektroforesis gel 2.Cari lebih banyak lagi di: http://muhammadhabibielecture.blogspot.com/2015/02/materi-kuliah-semester-4.html
ISOELECTRIC FOCUSING
Isoelectric focusing is a technique that separates molecules like proteins based on their isoelectric point, which is the pH at which the molecule has no net charge. It was developed in the 1960s and allows for much better resolution than older techniques. The process involves creating an immobilized pH gradient using carrier ampholytes, loading protein samples, and applying an electric field to cause proteins to migrate to the point in the gradient matching their isoelectric point. The separated proteins can then be visualized through staining. Isoelectric focusing is useful for applications like identifying serum proteins and aiding in proteomics research.
Gel Electrophoresis
Gel electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids based on their size and charge. It involves placing the molecules in an agarose, starch or polyacrylamide gel and applying an electric current, causing the molecules to migrate through the gel at different rates. SDS-PAGE is a common type of gel electrophoresis where sodium dodecyl sulfate is used to denature proteins, allowing separation based on molecular weight. The separated molecules can then be visualized by staining techniques to analyze proteins, detect mutations, and more.
PROTEIN ANALYSIS
PROTEIN ANALYSIS
SDS-PAGE (SDS-polyacrylamide gel electrophoresis)
Isoelectric focussing
High-performance liquid chromatography (HPLC)
Thin-layer chromatography (TLC)
Two-dimensional (2-D) gel electrophoresis
Identification of proteins by 2D gel
Protein identification by 2D gels uses a combination of isoelectric focusing (IEF) and SDS-PAGE. In IEF, proteins are separated based on their isoelectric point using an acrylamide gel containing an ampholyte pH gradient established by an electric current. Next, SDS-PAGE further separates the proteins by size. Finally, the proteins are visualized after staining, allowing identification by their position on the 2D gel based on isoelectric point and molecular weight.
Gel electrophorosis final
Gel electrophoresis is a method used to separate biomolecules like DNA, RNA, and proteins based on their size and charge. It works by applying an electric current to move the negatively charged molecules through a gel, with smaller molecules moving faster through the gel pores than larger ones. Common types of gels used include agarose for separating DNA, polyacrylamide for proteins, and starch for some protein analysis. The document provides details on how gel electrophoresis is performed and its applications in fields like forensics, molecular biology, and biochemistry.
Gel electrophoresis
Gel electrophoresis is a technique used to separate biomolecules like proteins, nucleic acids, and other charged molecules. It works by applying an electric field to move these charged molecules through a gel based on their size and charge. There are different types of gels used like agarose, polyacrylamide, and starch depending on the size of molecules to be separated. Samples are loaded into wells in the gel and an electric current is applied causing molecules to migrate through the gel at different rates. The separated biomolecules can then be visualized based on properties like fluorescence or staining to analyze differences in molecular weights and sizes. Gel electrophoresis has many applications in fields like forensics, molecular biology, genetics, and biochemistry
Applied Biochemistry
Electrophoresis is a technique used to separate charged molecules like proteins and nucleic acids based on their size and charge. It involves applying an electric field to move molecules through a medium like agarose gel or capillary. Shorter/less charged molecules move faster and are separated from longer/more charged molecules. It is used in laboratories and clinical settings to analyze biological samples and diagnose conditions.
2 d gel electrophoresis
This document summarizes a seminar presentation on 2D electrophoresis. 2D electrophoresis is a technique used to separate mixed proteins based on their isoelectric point and mass. It involves two sequential electrophoretic steps: iso-electric focusing to separate proteins by charge, followed by SDS-PAGE to separate by molecular weight. The document describes the principles, methods, applications and references for 2D electrophoresis.
2 d gel electrophoresis
Separation and identification of proteins in a sample by displacement in 2 dimensions oriented at right-angle to one another.
Gel electrophoresis
The document provides information on gel electrophoresis techniques. It discusses different types of gels like agarose, polyacrylamide, and starch that can be used for electrophoresis. Agarose gel is commonly used to separate macromolecules like nucleic acids and proteins due to its large pore size. Polyacrylamide gel is used to separate smaller molecules and provides better resolution than agarose. SDS-PAGE allows separation based on molecular weight by making all proteins negatively charged. The document outlines the procedures for agarose and polyacrylamide gel electrophoresis and their applications in analyzing proteins and nucleic acids.
Electrophoresis
This document discusses various types of electrophoresis techniques. It begins by explaining that electrophoresis involves charged molecules like proteins and nucleic acids migrating in response to an electrical field. It then discusses different gel types like agarose and polyacrylamide gels that are used as supporting matrices. It also covers techniques like SDS-PAGE, isoelectric focusing, two-dimensional gel electrophoresis, and capillary electrophoresis. The document provides details on how each technique separates molecules based on properties like size, charge, and isoelectric point.
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The protein samples are labeled with fluorescent dyes and then separated by 2D-PAGE.
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L’électrophorèse en champ pulsé est le résultat de la combinaison d’une digestion par des enzymes de restriction à faible nombre de sites de coupure et d’une électrophorèse adaptée à la grande taille des produits de digestion. Le résultat est un profil de restriction intéressant tout le génome du microorganisme
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Pulsed field gel electrophoresis (PFGE) is a technique used to separate large DNA, RNA, or protein molecules by periodically changing the direction of an electric field applied to a gel matrix. Conventional gel electrophoresis can only separate DNA fragments up to 50 kilobase pairs (kb) in size, while PFGE can separate molecules from a few kb to over 10 megabase pairs. PFGE applies alternating electric fields at different angles over time intervals to allow separation of very large biomolecules. It has applications in genome mapping, fingerprinting of organisms, and constructing yeast artificial chromosome libraries.
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Gel electrophoresis is a method used to separate biomolecules like DNA, RNA, and proteins based on their size and charge. There are two main types of gels used: agarose gels separate larger DNA and RNA fragments, while polyacrylamide gels are better for separating smaller proteins. DNA or proteins are loaded onto the gel and an electric current is applied, causing the molecules to migrate through the gel at different rates depending on their size and charge. The results can then be visualized to analyze samples.
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Electrophoresis and its application
Electrophoresis:
Electrophoresis is separation technique based on movement of charge particle in an electric field.
Movement of charge particles can be determined by following formula--
V= Eq/f
Where,
V= Velocity of the charged particle;
E= electric field of the molecule;
q= Net charge of the molecule; and
f= Frictional co-efficient of the molecule
Types of electrophoresis:
1. Agarose gel electrophoresis ;
2. Poly-acryl amide gel electrophoresis [PAGE];
3. Sodium do-decyl sulphate Poly- acrylamide gel electrophoresis [SDS-PAGE] ;
4. Two dimensional –Poly-acrylamide gel electrophoresis [2D-PAGE];
5. Pulse field gel electrophoresis [PFGE];
6. Capillary gel electrophoresis [CGE]; and
7. Disc electrophoresis for Protein.
Application of electrophoresis:
1. Estimation of the DNA molecule.[ Agarose , PAGE ]
2. Analysis of PCR product. [ Agarose ]
3. Separation of restricted genomic DNA and RNA. [Agarose and PAGE respectively]
4. Conformation of newly isolated DNA .[Agarose]
5. Separation of most small fragments of DNA. [PAGE]
6. In forensic science.[Agarose , PAGE, SDS-PAGE, 2D PAGE ,Capillary gel electrophoresis , PFGE]
8. In determining molecular wt. of protein.[SDS-PAGE].etc
Global analysis of protein by kk sahu sir
INTRODUCTION
GEL ELECTROPHORESIS
PRINCIPLE
BASIC CONCEPT
SUPPORT MEDIA
BUFFERS
APPARATUSS
AGE
PAGE
SDSPAGE
APPLICATIONS
CONCLUSIONS
BIBLIOGRAPHY
Electrophoresis and its types and its importance in Genetic engineering
This document discusses electrophoresis, which is a technique used to separate biomolecules like DNA, RNA, and proteins based on their size and charge. It moves through two common media - agarose gel and polyacrylamide gel. Agarose gel is used for larger molecules while polyacrylamide gel provides better resolution for smaller molecules. The document explains the principles, factors affecting separation, different types like agarose gel electrophoresis and polyacrylamide gel electrophoresis. It also discusses the requirements, steps involved and applications of agarose and polyacrylamide gel electrophoresis.
gel electrophoresis by Suresh B I
This document provides an introduction to gel electrophoresis. Gel electrophoresis is a method used to separate molecules like proteins and nucleic acids based on physical characteristics like size, shape, and charge. It works by applying an electric field to move molecules through a gel matrix. There are different types of gels that can be used like agarose or polyacrylamide. The document discusses the basic procedure, which involves applying samples to a gel, running an electric current, staining to visualize the separated molecules, and analyzing the results. Applications of gel electrophoresis include determining DNA fragment sizes, solving criminal cases or determining paternity or species relationships.
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* Registration is currently open *
Call for Research Papers!!!
Free – Extended Paper will be published as free of cost.
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July 13 ~ 14, 2024, Virtual Conference
Webpage URL: https://aiad2024.org/index
Submission Deadline: June 22, 2024
Submission System URL:
https://aiad2024.org/submission/index.php
Contact Us:
Here's where you can reach us : aiad@aiad2024.org (or) aiadconference@yahoo.com
WikiCFP URL: http://wikicfp.com/cfp/servlet/event.showcfp?eventid=180509©ownerid=171656
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2 d electrophoresis
- 1. TWO –DIMENSIONAL PROTEIN ELECTROPHORESIS By, RAHUL GHALME B.Tech. (Chemical Engineering)
- 2. Introduction Introduction by O'Farrell and Klose in 1975 Also known as ◦ 2-DE ◦ 2-D electrophoresis ◦ Two dimensional gel electrophoresis. Excellent resolution Form of gel electrophoresis Separation of mixed proteins
- 3. Basis for Separation Series combination of two electrophoretic separations Based on 1. Charge, using isoelectric focusing 2. Size
- 4. Procedure Place the sample in gel with pH gradient Apply potential difference across it
- 5. Detection Of Proteins Using chemical stains like ◦ Silver ◦ Coomassie Brilliant Blue 2D gel analysis software ◦ BioNumerics 2D, Delta2D, ◦ ImageMaster ◦ PDQuest, Progenesis, ◦ Melanie
- 6. Uses Analyze proteins Separation of proteins Excellent resolution To determine amino acid sequence Separation of DNA
- 7. Thank You