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A peptide corresponding to the N‐terminal 13 residues of T4 lysozyme forms an α‐helix
Author(s) -
McLeish Michael J.,
Nielsen Katherine J.,
Wade John D.,
Craik David J.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81187-5
Subject(s) - lysozyme , peptide , chemistry , micelle , two dimensional nuclear magnetic resonance spectroscopy , helix (gastropod) , crystallography , stereochemistry , biochemistry , aqueous solution , biology , ecology , snail
Solid‐phase methods have been used to synthesize LYS(1–13), a peptide corresponding to the first 13 residues of T4 lysozyme. 2D 1 H NMR techniques were used to investigate its solution structure in the presence of SDS micelles. The identification of numerous medium‐range NOESY crosspeaks and several slowly exchanging NH protons indicated the presence of an α‐helical structure. This was confirmed by simulated annealing calculations performed using XPLOR.