Lecture 5and6 - PRIMARY STRUCTURE OF PROTEINS Linking of...

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Unformatted text preview: PRIMARY STRUCTURE OF PROTEINS Linking of two amino acids via peptide bond is accompanied by loss of water Linkage is between α-carboxyl group of one amino acid with α-amino group of another amino acid Peptide bonds are kinetically stable (years) A series of amino acids joined by peptide bonds form a polypeptide chain PRIMARY STRUCTURE OF PROTEINS A polypeptide chain has polarity – positively charged N-terminal end and negatively charged C-terminal end The polypeptide backbone is regularly repeating and has H-bonding potential The variable side chains impart biological properties to polypeptides Each protein has a unique, precisely defined amino acid sequence specified by its gene nucleotide sequence PRIMARY STRUCTURE OF PROTEINS The peptide bond is essentially planar due to considerable double-bond character Free rotation about C=N bond is not possible, constraining conformation of the peptide backbone Free rotation about the other two bonds in peptide is allowed Rigid no rotation free rotation free rotation PRIMARY STRUCTURE OF PROTEINS...
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This note was uploaded on 05/05/2011 for the course BIOL 400 taught by Professor Dr.biology during the Spring '11 term at University of Tennessee.

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Lecture 5and6 - PRIMARY STRUCTURE OF PROTEINS Linking of...

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