BME 20100 Chapter Notes - Chapter 3.4: Electrospray Ionization, Edman Degradation, N-Terminus

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Covalent bonds (mainly peptide and disulfide bonds) linking amino acids. Recurring structures of amino acids, stable arrangements. 2 or more polypeptide units arranged together. Function of a protein depends on its amino acid sequence. Different protein function, different amino acid sequence. Defects in protein can range from single chance in sequence to deletion of whole. Polymorphic: sequence variants in human population polypeptide. Amino acid sequences of millions of proteins have been determined. Watson and crick deduced double helical structure. Labels and removes only amino-terminal residue from peptide. Used to identify protein with known sequence. Steps in protein sequencing which the carbonyl group is contributed by either lys or arg. Proteases: enzymes that catalyze hydrolytic cleavage in peptide bonds. Trypsin: digestive enzyme catalyzes hydrolysis of only those peptide bonds in. Polypeptide with 3 lys/arg yields 4 smaller peptides on cleavage with. Only used on proteins that have enough lys and arg trypsin.

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