The document discusses the 20 standard amino acids that make up proteins. It covers the common structures of amino acids including the alpha carbon, acid group, amino group, and side chain. It also classifies the 20 amino acids based on the properties of their side chains, including nonpolar, aromatic, polar uncharged, negatively charged and positively charged groups. Key amino acid properties and the single letter abbreviations used to represent each one are also outlined.
Amino Acids (building blocks of protein).pptxDr. Asif Anas
Classification on the bases of polarity
1. Non-polar amino acid with
Glycine, Alanine, Valine, Methionine, Leucine, Isoleucine, Proline, Phenylalanine, Tryptophan.
2. Polar Amino Acids
I. Negatively charge amino acid
Aspartic acid, Glutamic Acid
II. Positively charge amino acid
Lysine, Arginine, Histidine.
III. Neutral amino acid
Serine, Threonine, Asparagine, Glutamine, Cysteine, Tyrosine
Polarity of amino acid
Tyr>Ser>Asp>Glu>Asn>Gln>Arg
Non-polarity of amino acid
Phy>Ala>Val>Gly>Leu>Cys
Which amino acid is hydrophobic?
Which amino acid is hydrophilic?
Which of the amino acids residues are most likely to be found in the interior of the water soluble protein?
Classification of amino acids
Neutral amino acids
Glycine-Gly-G
Amino acid with smallest side chain
Most abundant in collagen
No chiral carbon (No optical activity)
Sweet in taste
Neurotransmitter inhibitor
2. Alanine-Ala-A
Amino acid with methyl group
Most abundant amino acid in protein
3. Valine-Val-V
Branched at β-carbon
Amino Acid with two chiral carbon
4. Leucine-Leu-L
Branched at γ-carbon
5. Isoleucine-Ile-I
Amino acid with 2 chiral carbon
6. Serine-Ser-S
Help in the synthesis of muscle protein
Phosphorylation in cell signaling
7. Threonine-Thr-T
Branched at β-carbon
Amino Acid with two chiral carbon
8. Proline-Pro-P
A cyclic imino acid
Present in α-helix and β-turn
Acidic amino acids
9. Aspartic acid-Asp-D
Amino acid with β-carbonyl group
Frequently present on N-terminus of α-helix
10. Glutamic Acid-Glu-E
Amide form of acidic amino acids
11. Asparagine-Asn-N
12. Glutamine-Gln-Q
Sulphur containing amino acids
13. Cysteine-Cys-C
Amino acid with thiol group
Involve in disulphide bond
14. Methionine-Met-M
First amino acid in protein
Second least present in protein
Basic amino acids
15. Histidine-His-H
Amino acid with imidazole ring
Having buffering capacity
Help in Immune response
16. Lysine-Lys-K and 17. Arginine-Arg-R
Rich in histone protein
Lysine has butyl-ammonium side chain
Aromatic ring acidic amino acids
18. Phenylalanine-Phe-F
Maximum absorption at 280nm
Naturally present in breast milk
Related with phenylketonuria
19. Tyrosine-Tyr-Y
Maximum absorption at 280nm
Phosphorylation in cell signaling
20. Tryptophan-Trp-W
Least present in protein, indole ring amino acid
General Characters of amino acids
There are more than 500 amino acids present in the nature.
Only 20+2 participate in the formation proteins.
Amino acids have N-terminus, C-terminus and R-group in their structure.
Average mass of an amino acid residue is ~ 110 Da.
Selenocystine is 21st amino acid, analog of cysteine, having antioxidant acitivity.
Pyrolysisne is not present in human.
Amino acids are made visible on the chromatogram by the treatment with ninhydrin.
Non-polar amino acid are found mostly in the core of protein.
Acid base characters of amino acids
pK can be defined as the pH at which the acid is 50% dissociated.
If- pK=pH+1………….. Acid is 91% dissociated.
pK=pH+2………….. Acid is 99%
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
Amino acids are the building blocks of proteins and thus a code of life. This slide discusses about the structure, importance and various classifications of amino acids.
Amino acids structure classification & function by KK Sahu sirKAUSHAL SAHU
INTRODUCTION
STRUCTURE
CLASSIFICATION OF AMINO ACIDS
ELEROCHEMICAL PROPERTIES
IONIZATION
TITRATION CURVE
NONSTANDARD PROTEIN AMINO ACIDS
NONPROTEIN AMINO ACIDS
DISTRIBUTION IN PROTEIN
ESSENTIAL AMINO ACIDS
FUNCTIONS
Chemistry of amino acids with their clinical applicationsrohini sane
A comprehensive presentation on Chemistry of Amino acids with their clinical applications for MBBS , BDS, B Pharm & Biotechnology students to facilitate easy- learning.
Amino Acids (building blocks of protein).pptxDr. Asif Anas
Classification on the bases of polarity
1. Non-polar amino acid with
Glycine, Alanine, Valine, Methionine, Leucine, Isoleucine, Proline, Phenylalanine, Tryptophan.
2. Polar Amino Acids
I. Negatively charge amino acid
Aspartic acid, Glutamic Acid
II. Positively charge amino acid
Lysine, Arginine, Histidine.
III. Neutral amino acid
Serine, Threonine, Asparagine, Glutamine, Cysteine, Tyrosine
Polarity of amino acid
Tyr>Ser>Asp>Glu>Asn>Gln>Arg
Non-polarity of amino acid
Phy>Ala>Val>Gly>Leu>Cys
Which amino acid is hydrophobic?
Which amino acid is hydrophilic?
Which of the amino acids residues are most likely to be found in the interior of the water soluble protein?
Classification of amino acids
Neutral amino acids
Glycine-Gly-G
Amino acid with smallest side chain
Most abundant in collagen
No chiral carbon (No optical activity)
Sweet in taste
Neurotransmitter inhibitor
2. Alanine-Ala-A
Amino acid with methyl group
Most abundant amino acid in protein
3. Valine-Val-V
Branched at β-carbon
Amino Acid with two chiral carbon
4. Leucine-Leu-L
Branched at γ-carbon
5. Isoleucine-Ile-I
Amino acid with 2 chiral carbon
6. Serine-Ser-S
Help in the synthesis of muscle protein
Phosphorylation in cell signaling
7. Threonine-Thr-T
Branched at β-carbon
Amino Acid with two chiral carbon
8. Proline-Pro-P
A cyclic imino acid
Present in α-helix and β-turn
Acidic amino acids
9. Aspartic acid-Asp-D
Amino acid with β-carbonyl group
Frequently present on N-terminus of α-helix
10. Glutamic Acid-Glu-E
Amide form of acidic amino acids
11. Asparagine-Asn-N
12. Glutamine-Gln-Q
Sulphur containing amino acids
13. Cysteine-Cys-C
Amino acid with thiol group
Involve in disulphide bond
14. Methionine-Met-M
First amino acid in protein
Second least present in protein
Basic amino acids
15. Histidine-His-H
Amino acid with imidazole ring
Having buffering capacity
Help in Immune response
16. Lysine-Lys-K and 17. Arginine-Arg-R
Rich in histone protein
Lysine has butyl-ammonium side chain
Aromatic ring acidic amino acids
18. Phenylalanine-Phe-F
Maximum absorption at 280nm
Naturally present in breast milk
Related with phenylketonuria
19. Tyrosine-Tyr-Y
Maximum absorption at 280nm
Phosphorylation in cell signaling
20. Tryptophan-Trp-W
Least present in protein, indole ring amino acid
General Characters of amino acids
There are more than 500 amino acids present in the nature.
Only 20+2 participate in the formation proteins.
Amino acids have N-terminus, C-terminus and R-group in their structure.
Average mass of an amino acid residue is ~ 110 Da.
Selenocystine is 21st amino acid, analog of cysteine, having antioxidant acitivity.
Pyrolysisne is not present in human.
Amino acids are made visible on the chromatogram by the treatment with ninhydrin.
Non-polar amino acid are found mostly in the core of protein.
Acid base characters of amino acids
pK can be defined as the pH at which the acid is 50% dissociated.
If- pK=pH+1………….. Acid is 91% dissociated.
pK=pH+2………….. Acid is 99%
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
Amino acids are the building blocks of proteins and thus a code of life. This slide discusses about the structure, importance and various classifications of amino acids.
Amino acids structure classification & function by KK Sahu sirKAUSHAL SAHU
INTRODUCTION
STRUCTURE
CLASSIFICATION OF AMINO ACIDS
ELEROCHEMICAL PROPERTIES
IONIZATION
TITRATION CURVE
NONSTANDARD PROTEIN AMINO ACIDS
NONPROTEIN AMINO ACIDS
DISTRIBUTION IN PROTEIN
ESSENTIAL AMINO ACIDS
FUNCTIONS
Chemistry of amino acids with their clinical applicationsrohini sane
A comprehensive presentation on Chemistry of Amino acids with their clinical applications for MBBS , BDS, B Pharm & Biotechnology students to facilitate easy- learning.
The Roman Empire A Historical Colossus.pdfkaushalkr1407
The Roman Empire, a vast and enduring power, stands as one of history's most remarkable civilizations, leaving an indelible imprint on the world. It emerged from the Roman Republic, transitioning into an imperial powerhouse under the leadership of Augustus Caesar in 27 BCE. This transformation marked the beginning of an era defined by unprecedented territorial expansion, architectural marvels, and profound cultural influence.
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Under Augustus, the empire experienced the Pax Romana, a 200-year period of relative peace and stability. Augustus reformed the military, established efficient administrative systems, and initiated grand construction projects. The empire's borders expanded, encompassing territories from Britain to Egypt and from Spain to the Euphrates. Roman legions, renowned for their discipline and engineering prowess, secured and maintained these vast territories, building roads, fortifications, and cities that facilitated control and integration.
The Roman Empire’s society was hierarchical, with a rigid class system. At the top were the patricians, wealthy elites who held significant political power. Below them were the plebeians, free citizens with limited political influence, and the vast numbers of slaves who formed the backbone of the economy. The family unit was central, governed by the paterfamilias, the male head who held absolute authority.
Culturally, the Romans were eclectic, absorbing and adapting elements from the civilizations they encountered, particularly the Greeks. Roman art, literature, and philosophy reflected this synthesis, creating a rich cultural tapestry. Latin, the Roman language, became the lingua franca of the Western world, influencing numerous modern languages.
Roman architecture and engineering achievements were monumental. They perfected the arch, vault, and dome, constructing enduring structures like the Colosseum, Pantheon, and aqueducts. These engineering marvels not only showcased Roman ingenuity but also served practical purposes, from public entertainment to water supply.
Welcome to TechSoup New Member Orientation and Q&A (May 2024).pdfTechSoup
In this webinar you will learn how your organization can access TechSoup's wide variety of product discount and donation programs. From hardware to software, we'll give you a tour of the tools available to help your nonprofit with productivity, collaboration, financial management, donor tracking, security, and more.
Embracing GenAI - A Strategic ImperativePeter Windle
Artificial Intelligence (AI) technologies such as Generative AI, Image Generators and Large Language Models have had a dramatic impact on teaching, learning and assessment over the past 18 months. The most immediate threat AI posed was to Academic Integrity with Higher Education Institutes (HEIs) focusing their efforts on combating the use of GenAI in assessment. Guidelines were developed for staff and students, policies put in place too. Innovative educators have forged paths in the use of Generative AI for teaching, learning and assessments leading to pockets of transformation springing up across HEIs, often with little or no top-down guidance, support or direction.
This Gasta posits a strategic approach to integrating AI into HEIs to prepare staff, students and the curriculum for an evolving world and workplace. We will highlight the advantages of working with these technologies beyond the realm of teaching, learning and assessment by considering prompt engineering skills, industry impact, curriculum changes, and the need for staff upskilling. In contrast, not engaging strategically with Generative AI poses risks, including falling behind peers, missed opportunities and failing to ensure our graduates remain employable. The rapid evolution of AI technologies necessitates a proactive and strategic approach if we are to remain relevant.
Biological screening of herbal drugs: Introduction and Need for
Phyto-Pharmacological Screening, New Strategies for evaluating
Natural Products, In vitro evaluation techniques for Antioxidants, Antimicrobial and Anticancer drugs. In vivo evaluation techniques
for Anti-inflammatory, Antiulcer, Anticancer, Wound healing, Antidiabetic, Hepatoprotective, Cardio protective, Diuretics and
Antifertility, Toxicity studies as per OECD guidelines
Honest Reviews of Tim Han LMA Course Program.pptxtimhan337
Personal development courses are widely available today, with each one promising life-changing outcomes. Tim Han’s Life Mastery Achievers (LMA) Course has drawn a lot of interest. In addition to offering my frank assessment of Success Insider’s LMA Course, this piece examines the course’s effects via a variety of Tim Han LMA course reviews and Success Insider comments.
Operation “Blue Star” is the only event in the history of Independent India where the state went into war with its own people. Even after about 40 years it is not clear if it was culmination of states anger over people of the region, a political game of power or start of dictatorial chapter in the democratic setup.
The people of Punjab felt alienated from main stream due to denial of their just demands during a long democratic struggle since independence. As it happen all over the word, it led to militant struggle with great loss of lives of military, police and civilian personnel. Killing of Indira Gandhi and massacre of innocent Sikhs in Delhi and other India cities was also associated with this movement.
14. -C-C-CONH 2 -C-CONH 2 -C-COOH -C-C-COOH -H -CH 3 -C-OH -C-SH -C-C-S-C -C-C-C-C-NH 3 + 雙 和 線 環狀線 中央線 南 港 線 中 山 線 西 北 線 Aliphatic Amide Acidic Imino, Circular Basic Sulfur Hydroxy Aromatic 胺基酸地下鐵道圖 Juang RH (2004) BCbasics Leu L P Pro -C-C C N N + -C- -C- -OH -C- N -C-C-C-N-C-N N + = C -C-C-C C -C-C-C C C -C C C C HN C-COOH -C-C OH Gln Q Asn N Asp D Glu E Phe F Arg R Lys K His H Gly G A A Ala V Val I Ile Y Tyr Ser S Thr T Met M Cys C Trp W Non-polar Polar
15. If only one amino acid (a.a.) begins with a certain letter, that letter is used Cys teine = Cys = C His tidine = His = H I so le ucine = Ile = I Met hionine = Met = M Ser ine = Ser = S Val ine = Val = V Key convention, p. 74
16. If more than one a.a. begins with a certain letter, that letter is assigned to the most commonly occurring one Ala nine = Ala = A Gly cine = Gly = G Leu cine = Leu = L Pro line = Pro = P Thr eonine = Thr = T
17. Phonetically suggestive Asp artic acid (“aspar D ic acid”) = Asp = D Phe nylalanine (“ F enylalanine”) = Phe = F Arg inine (“a R ginine”) = Arg = R Tyr osine (“t Y rosine”) = Tyr = Y Tr y p tophan ( double ring in the molecule) = Trp = W
18. A letter close to the initial is used As paragine (contains N ) = As n = N Glu tamic acid (near D) = Glu = E Gl utami n e (“Q-tamine”) = Gl n = Q Lys ine (near L) = Lys = K