Title : Nuclear-magnetic-resonance-spectroscopic studies of the amino groups of insulin.

Pub. Date : 1977 Jun 15

PMID : 19247






5 Functional Relationships(s)
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1 By difference spectroscopy it is possible to follow the shift with pH of the epsilon-CH2 and delta-CH2 proton resonances of lysine-B29 in insulin. Lysine insulin Homo sapiens
2 In methylated insulin the dimethyl proton resonances of glycine-A1, phenylalanine-B1 and lysine-B29 can be followed as a function of pH. Lysine insulin Homo sapiens
3 In native insulin pKapp values of 6.7 and 8.0 are obtained for phenylalanine-B1 and glycine-A1 (the assignment is tentative) and 11.2 for lysine-B29. Lysine insulin Homo sapiens
4 Separate resonances have been observed from the lysine-B29 Nepsilon-(CH3)2 group for the monomeric and dimeric forms of methylated insulin, which indicates a small change in the environment of lysine-B29 on dimerisation. Lysine insulin Homo sapiens
5 Separate resonances have been observed from the lysine-B29 Nepsilon-(CH3)2 group for the monomeric and dimeric forms of methylated insulin, which indicates a small change in the environment of lysine-B29 on dimerisation. Lysine insulin Homo sapiens