A peptide corresponding to the N‐terminal 13 residues of T4 lysozyme forms an α‐helix

[摘要]

Solid-phase methods have been used to synthesize LYS(1–13), a peptide corresponding to the first 13 residues of T4 lysozyme. 2D ¹H 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.

[学科分类] 生物化学/生物物理

[关键词] Nuclear magnetic resonance;Protein folding;Peptide fragment;T4 lysozyme;Peptide conformation;BPTI;bovine pancreatic trypsin inhibitor;RNAse A;ribonuclease A;NMR;nuclear magnetic resonance;Fmoc;fluorenyl methyloxycarbonyl;SDS;sodium dodecyl sulphate;NOESY;nuclear Overhauser enhancement spectroscopy;TOCSY;total correlation spectroscopy;DQF-COSY;double quantum filtered correlation spectroscopy;FID;free induction decay.