- Amino acids are the building blocks of proteins and consist of an amino group, a carboxyl group, and a side chain specific to each amino acid. There are 20 standard amino acids used in protein synthesis.
- Amino acids can be classified based on the polarity of their side chains as neutral and nonpolar, neutral and polar, basic and polar, or acidic and polar. They play important roles in the body such as enzyme catalysis.
- Proteins are formed via peptide bonds between amino acids. Chains of up to 50 amino acids are called polypeptides while longer chains are proteins. Important proteins include hormones like insulin which regulates blood sugar levels.
AMINO ACIDS ARE THE BUILDING BLOCK OF PROTEIN MOLECULES.AMIINO ACIDS HAVE THE COMMON STRUCTURE WITH A CARBOXYLIC GROUP AND A NH2 GROUP ALONG WITH A VARIABLE R GROUP(SIDE CHAIN).THEY ARE CLASSIFIED INTO POLAR ,NON POLAR,ACIDIC AND BASIC GROUPS.BASED ON THIS DIFFERENT AMINO ACIDS HAVE DIFFERENT PROPERTIES.
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
Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide...ShwetaMishra115
Descriptive notes on polypeptides
Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide
AMINO ACIDS ARE THE BUILDING BLOCK OF PROTEIN MOLECULES.AMIINO ACIDS HAVE THE COMMON STRUCTURE WITH A CARBOXYLIC GROUP AND A NH2 GROUP ALONG WITH A VARIABLE R GROUP(SIDE CHAIN).THEY ARE CLASSIFIED INTO POLAR ,NON POLAR,ACIDIC AND BASIC GROUPS.BASED ON THIS DIFFERENT AMINO ACIDS HAVE DIFFERENT PROPERTIES.
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
Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide...ShwetaMishra115
Descriptive notes on polypeptides
Polypeptides,peptides, types of peptides, structure of dipeptide, tripeptide and oligopeptide and different functions of peptide
Table of Contents
What are Amino Acids?
Properties of Amino acids
Physical Properties
Chemical Properties
Structure of Amino acids
Classification of amino acids on the basis of R-group
Classification of amino acids on the basis of nutrition
Essential amino acids (Nine)
Non-essential amino acids (Eleven)
Classification of amino acids on the basis of the metabolic fate
Functions of Amino acids
this ppt covers about amino acids, classification, protein ,classifications, structure, denaturation, structure & fnctional relationship with applied aspects.
Biomolecules Proteins and Amino Acids.pptxSejalWasule
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This PPTX is a basic presentation of a short sight of 10 minutes, about what role, classification & properties of amino acids, Protein organization, functions of proteins
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1. Amino Acids
Dr.B.RENGESH | M.Tech., Ph.D.
Associate Professor, Department of Pharmaceutical Technology,
Mahendra Engineering College (Autonomous),
Namakkal District, Tamil Nadu, India
2. PROTEINS
v Proteins (Greek proteios, “primary” or “of first importance”) are
biomolecules consisting of polypeptides joined by peptide bonds between
the amino and carboxyl groups of amino acid residues.
v Proteins perform many vital functions:
– Enzymes as biochemical catalysts.
– Many proteins have structural or mechanical functions.
– Proteins are important in cell signaling, immune responses, cell
adhesion, and the cell cycle.
– Proteins are a necessary component in animal diets.
3. AMINO ACIDS
v There are more than 300 amino acids that occur in nature and many are yet
to be characterized.
v Only 20 of the amino acids are found in the protein structure and the
genetic code exists for only the 20 amino acids.
v These amino acids are called alpha (α)-amino acids because the amino
group is attached to the first carbon in the chain connected to the carboxyl
carbon.
4. AMINO ACIDS
v The amino acids are classified by the polarity of the R group side chains,
and whether they are acidic or basic:
– neutral, nonpolar
– neutral, polar
– basic, polar (contains an additional amino group)
– acidic, polar (contains an additional carboxylate group)
v All of the amino acids are also known by a three-letter and one-letter
abbreviations
5. AMINO ACIDS – Name and Abbreviations
Name 3-letter abbreviation 1-letter abbreviation
Alanine Ala A
Arginine Arg R
Asparagine Asn N
Aspartic acid Asp D
Cysteine Cys C
Glutamic acid Glu E
Glutamine Gln Q
Glycine Gly G
Histidine His H
Isoleucine Ile I
6. AMINO ACIDS – Name and Abbreviations
Name 3-letter abbreviation 1-letter abbreviation
Leucine Leu L
Lysine Lys K
Methionine Met M
Phenylalanine Phe F
Proline Pro P
Serine Ser S
Threonine Thr T
Tryptophan Trp W
Tyrosine Tyr Y
Valine Val V
7. AMINO ACIDS – classification – Neutral, Non-polar side chains
8. AMINO ACIDS – classification – Neutral, Polar side chains
9. AMINO ACIDS – classification – Basic, Polar side chains
10. AMINO ACIDS – classification – Acidic, Polar side chains
11. AMINO ACIDS – Nutritional Classification
v Essential amino acids – These amino acids cannot be formed (synthesized) in the body
and so, it is essential to be included in the diet.
1. Valine 2. Isoleucine 3. Lysine 4. Leucine
5. Methionine 6. Tryptophan 7. Threonine 8. Phenyl alanine
v Non-essential amino acids – The amino acids that can be synthesized in the body by
regular metabolism in enough amounts. They need not be included in the diet.
1. Glycine 2. Alanine 3. Cysteine 4. Tyrosine
5. Proline 6. Serine 7. Asparagine 8. Glutamine
9. Aspartic acid 10. Glutamic acid
v Semi-essential amino acids – These amino acids are formed in the body but not in
sufficient amount for body requirements especially in children.
1. Arginine 2. Histidine
12. AMINO ACIDS – Zwitterions
v Because amino acids contain both an acidic and a basic functional group,
an internal acid-base reaction occurs, forming an ion with both a positive
and a negative charge called a zwitterion
13. AMINO ACIDS – Zwitterions @ solutions – Structure changes
v Lowering the pH of the solution causes the zwitterion to pick up a proton
v Increasing the pH of the solution causes the zwitterion to lose a proton
14. AMINO ACIDS – Zwitterions - Properties
v Since the pH of the solution affects the charge on the amino acid, at some
pH, the amino acid will form a zwitterion. This is called the isoelectric
point.
v Each amino acid (and protein) has a characteristic isoelectric point: those
with neutral R groups are near a pH of 6, those with basic R groups have
higher values, and those with acidic R groups have lower values.
v Because amino acids can react with both H3O+ and OH-, solutions of
amino acids and proteins can act as buffers. (E.g., blood proteins help to
regulate the pH of blood.)
15. AMINO ACIDS – Reactions – Oxidation of Cysteine
v Cysteine is the only amino acid that contains a sulfhydryl (thiol, R—SH)
group. Thiols are easily oxidized to form disulfide bonds (R—S—S—R).
This allows cysteine to dimerize to form cystine
16. AMINO ACIDS – Reactions – Peptide Formation
v Amides formed from the reaction of an amine and a carboxylic acid
17. AMINO ACIDS – Reactions – Peptide Formation
v If 3rd AA join to form a tripeptide
18. PEPTIDES - terminologies
v A fourth amino acid would form a tetrapeptide, a fifth would form a
pentapeptide, and so on.
v Short chains are referred to as peptides, chains of up to about 50 amino acids
are polypeptides, and chains of more than 50 amino acids are proteins
v The residue with a free amino group is called the N-terminal residue, and is
written on the left end of the chain.
v The residue with a free carboxylate group is called the C-terminal residue, and
is written on the right end of the chain.
v Peptides are named by starting at the N-terminal end and listing the amino acid
residues from left to right. i.e. usually represented by their three-letter
abbreviations, separated by dashes. Eg. Gly-Ala (Gly = N-terminal, Ala = C-terminal)
20. Glucagon – Glycogen – Insulin
v Peptide hormone
produced by alpha
cells of the pancreas.
v Works to raise the
concentration of
glucose and fatty
acids in the
bloodstream
i.e., in response to
low concentration of
Insulin
v Peptide hormone
produced by beta cells of
the pancreas.
v It promotes the
absorption of
carbohydrates, especially
glucose from the blood
into liver, fat and skeletal
muscle cells.
v Converted into glycogen