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- W1506285852 abstract "Analysis of the 220 MHz proton magnetic resonance spectra of bovine neurophysins-I and -II and of the effects of pH and succinylation of these spectra has allowed identification of the -CH3 proton resonances of the amino-terminal alanine of both proteins and of the -CH3 resonances of methionine-2 of neurophysin-II. The alanine -CH3 resonance of neurophysin-I is a sharp doublet at all pH values between 1 and 10.5 indicating relatively few restrictions on its mobility. By contrast, the -CH3 resonances of the amino-terminal alanine and methionine-2 of neurophysin-II undergo pH-dependent changes in broadening compatible with the formation of an intramolecular salt-bridge at neutral pH between the protonated alpha-amino and an unprotonated side chain carboxyl. The results suggest that differeces in the properties of the two proteins are partially mediated by conformational differences involving their amino-terminal sequences. The potential usefulness of the amino-terminal resonances as n.m.r. 'reporter' signals is additionally demonstrated by studies of the effects of spin labels on the neurophysin-I amino-terminal alanine resonance; these studies place the amino-terminus of neurophysin-I approximately 14 A from residue 3 of peptides bound to the strong neurophysin hormone-binding site." @default.
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- W1506285852 date "2009-01-12" @default.
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- W1506285852 title "IDENTIFICATION AND OBSERVATION OF ALKYL PROTON RESONANCES OF THE AMINO-TERMINAL RESIDUES OF BOVINE NEUROPHYSINS" @default.
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- W1506285852 doi "https://doi.org/10.1111/j.1399-3011.1979.tb01851.x" @default.
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