The document discusses the monomer units that make up protein polymers. It states that long polypeptide chains of proteins are synthesized from L-amino acids and their derivatives. These amino acids participate in many cellular functions and short amino acid polymers called peptides function as hormones, hormone factors, and neurotransmitters in the neuroendocrine system. The document then goes on to describe the basic structure of amino acids and different ways of classifying them, such as by their side chain properties or metabolic roles. It provides examples to illustrate different amino acid categories.
The document discusses the monomer units that make up protein polymers. It states that long polypeptide chains of proteins are synthesized from L-amino acids and their derivatives. These amino acids participate in many cellular functions and short amino acid polymers called peptides function as hormones, hormone factors, and neurotransmitters in the neuroendocrine system. The document then goes on to describe the basic structure of amino acids and different ways of classifying them, such as by their side chain properties or metabolic roles. It provides examples to illustrate different amino acid categories.
The document discusses the monomer units that make up protein polymers. It states that long polypeptide chains of proteins are synthesized from L-amino acids and their derivatives. These amino acids participate in many cellular functions and short amino acid polymers called peptides function as hormones, hormone factors, and neurotransmitters in the neuroendocrine system. The document then goes on to describe the basic structure of amino acids and different ways of classifying them, such as by their side chain properties or metabolic roles. It provides examples to illustrate different amino acid categories.
The document discusses the monomer units that make up protein polymers. It states that long polypeptide chains of proteins are synthesized from L-amino acids and their derivatives. These amino acids participate in many cellular functions and short amino acid polymers called peptides function as hormones, hormone factors, and neurotransmitters in the neuroendocrine system. The document then goes on to describe the basic structure of amino acids and different ways of classifying them, such as by their side chain properties or metabolic roles. It provides examples to illustrate different amino acid categories.
Provide the monomer units from which the long polypeptide chains of proteins are synthesized
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L-amino acids and their derivatives participate in cellular functions as diverse as: Nerve transmission and the Biosynthesis of porphyrins, Purines, pyrimidines, and urea.
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Short polymers of amino acids called peptides perform prominent roles in the neuroendocrine system as : hormones, hormone-releasing factors, neuromodulators, or neurotransmitters.
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Each amino acid (except proline) has a carboxyl group, an amino group and a distinctive side chain bonded to the alpha carbon atom. At physiological pH the carboxyl group is dissociated forming the negatively charged carboxylate ion(-COO-), and the amino group is protonated(-NH3+)
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Amino acids can be classified in 4 ways: 1. Based on structure 2. Based on the side chain characters 3. Based on nutritional requirements 4. Based on metabolic fate
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1) Aliphatic amino acids They are classified in three broad categories: Mono amino mono carboxylic acids They are further subdivided in 5 groups: a. Simple amino acids-example: glycine, alanine b. Branched chain amino acids-e.g.: valine,leucine,isoleucine c. Hydroxyl group containing amino acids-e.g.: serine, threonine d. Sulphur containing amino acids-e.g.: cysteine, cystine, methionine e. Amide group containing amino acids-e.g.- asparagine,glutamine
A. Amino acids with a non-polar side-chain: e.g.: Alanine, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan, Proline
Each of these amino acids has a side chain that does
not bind or give off protons or participates in hydrogen or ionic bonds.
Side chains of these amino acids can be thought of as
“Oily” or lipid like, a property that promotes hydrophobic interactions.
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Namrata Chhabra 3/25/2017 21 e.g. Serine, Threonine, Tyrosine, Cysteine, Asparagine and Glutamine. These amino acids are uncharged at neutral pH, although the side chains of cysteine and Tyrosine can lose a proton at an alkaline pH. Serine , Threonine and Tyrosine each contains a polar hydroxyl group that can participate in hydrogen bond formation. Side chains of Asparagine and Glutamine contain a carbonyl group and amide group, they can also participate in hydrogen bond formation.
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Namrata Chhabra 3/25/2017 23 a) Amino acids with a positively charged side-chain: The basic amino acids- Lysine, Arginine and Histidine b) Amino acids with a negatively charged side-chain: The acidic amino acids- Glutamic acid and Aspartic acid They are hydrophilic in nature.
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Namrata Chhabra 3/25/2017 25 I. Essential amino acids: These amino acids cannot be synthesized in the body and have to be present essentially in the diet. Examples- Valine, Isoleucine, Leucine, Lysine, Methionine, Threonine, Tryptophan, and Phenylalanine.
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II. Semi-essential amino acids: These amino acids can be synthesized in the body but the rate of synthesis is lesser than the requirement(e.g. during growth, repair or pregnancy) Examples-Arginine and Histidine.
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Non-essential amino acids: III. These amino acids are synthesized in the body, thus their absence in the diet does not adversely affect the growth. Examples- Glycine, Alanine, and the other remaining amino acids.
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The carbon skeleton of amino acids can be used either for glucose production or for the production of ketone bodies, Based on that I.Both glucogenic and ketogenic amino acids: Isoleucine, Tyrosine, Phenylalanine and Tryptophan
Of the over 300 naturally occurring amino acids, 20 constitute the monomer units of proteins. These 20 amino acids are called the Primary or Standard amino acids. Selenocysteine is the 21st Amino Acid The other are Pyroglutamate and Pyrolysine.