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Steric hindrance glutamate

However, trypsin can not hydrolyze the lysine-proline bond (probably a result of steric hindrance), and if a protein sequence contains adjacent basic residues (KK, KR, RK or RR) the resulting digestion products include single amino acids (K or R) that are difficult to detect. As a check on this and other possibilities, other proteases are used in addition to trypsin, e.g., Lys-C, Arg-C and Glu-C are proteases that hydrolyze peptide bonds on the C-terminal side of only lysine, arginine and glutamic acid, respectively. Cyanogen bromide chemically hydrolyses peptide bonds on the C-terminal side of methionine to form peptides with a homoserine residue (X = -CH2-CH2-OH) at the C-terminus. [Pg.664]


See other pages where Steric hindrance glutamate is mentioned: [Pg.124]    [Pg.396]    [Pg.42]    [Pg.65]    [Pg.195]    [Pg.538]    [Pg.127]    [Pg.248]    [Pg.252]    [Pg.1136]    [Pg.20]    [Pg.537]    [Pg.1276]    [Pg.376]    [Pg.376]    [Pg.1082]    [Pg.1652]    [Pg.115]    [Pg.83]    [Pg.115]    [Pg.110]    [Pg.1377]    [Pg.129]    [Pg.39]   
See also in sourсe #XX -- [ Pg.239 , Pg.240 ]




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