Course review

B1.2 Proteins

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Learning objective

B1.2.1—Generalized amino acid structure

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• Amino acids have an alpha carbon bonded to an amine, carboxyl, hydrogen, and R-group • The R-group varies between amino acids and determines chemical properties • Proteins contain C, H, O, N, and usually S

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B1.2.2—Condensation reactions

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• Condensation joins the carboxyl group of one amino acid to the amine group of another • A peptide bond forms and water is released • Chains have an N-terminus and C-terminus and are assembled at ribosomes

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B1.2.3—Dietary amino acids

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• Essential amino acids cannot be synthesized and must be obtained from dietary protein • Non-essential amino acids can be made by transamination, mainly in the liver • Deficiency of essential amino acids limits protein synthesis and can cause malnutrition

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B1.2.4—Infinite variety of peptide chains

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• Twenty coded amino acids can form vast numbers of sequences • Protein diversity depends on amino acid type, number, and order • Genes encode polypeptide sequences; the proteome is the full protein set expressed

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B1.2.5—Effect of pH and temperature

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• Protein shape determines function, especially enzyme active sites • High temperature or unsuitable pH disrupts weak bonds and denatures proteins • Denaturation may be reversible in small proteins but often becomes irreversible

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