![]() In nutrition, amino acids are classified as either essential or non-essential. These amino acids must be supplied from an exogenous diet because the human body lacks the metabolic pathways required to synthesize these amino acids. H C N = O C = O Alpha helix Every C=O bonded to N-H 4 residues away forms a helix core is backbone R-groups outside 3.Essential amino acids, also known as indispensable amino acids, are amino acids that humans and other vertebrates cannot synthesize from metabolic intermediates. H H H _ _ _ _ H N1- C1- C1- N2- C2- C2- N3- C3- C3- OH = O O O R R R _ _ _ Secondary structure hydrogen bonding backbone groups H-bond donors H-bond acceptors -helix Two main secondary structures: -sheet Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala Phe-Val-Asn-Gln-His Gln-His-Leu-Cys Leu-Val-Glu-Ala His-Leu-Cys-Gly-Ser Gly-Ser-His-Leu-Val His-Leu-Val-Glu Primary structure study evolution -chain 146 residues horses - humans = 26 pigs - humans = 10 gorillas - humans = 1 1 successful change / 10,000,000 years Primary structure - selective hydrolysis ![]() Primary structure sequence of amino acids hemoglobin transports O2 and CO2 300 amino acids 4 protein chains Sickle cell anemia 6thamino acid from N-terminus Glu R Val -CH2CH2-CO2H -CH(CH3)2 water soluble water insoluble H H H _ _ _ = O O O R R R _ _ _ Polypeptides “backbone” _ H N1- C1- C1- N2- C2- C2- N3- C3- C3- OH peptide bonds C-terminal residue N-terminal residue biological activity = structure 4 levels protein structure Amino acids R-groups non-polar polar acidic basic proteins condensation between carboxylic acids and amines + + H2O carboxylic acid amide amineĪmides resonance structure amides dipeptide glycine alanine Ala-Gly +H2O
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