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

FEBS Letters

Wade, John D.²  McLeish, Michael J.¹  Nielsen, Katherine J.¹  Craik, David J.¹ 

[1] School of Pharmaceutical Chemistry, Victorian College of Pharmacy, 381 Royal Parade, Parkville, Vic. 3052, Australia;Howard Florey Institute, University of Melbourne, Parkville, Vic. 3052, Australia

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.;   

DOI  :  10.1016/0014-5793(93)81187-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown