Backbone folding of the polypeptide cardiac stimulant anthopleurin‐A determined by nuclear magnetic resonance, distance geometry and molecular dynamics

FEBS Letters

van Gunsteren, Wilfred F.¹  Mabbutt, Bridget C.²  Torda, Andrew E.²  Norton, Raymond S.² 

[1] Laboratory of Physical Chemistry, University of Groningen, Nijenborgh 16, 9747 AG, Groningen, The Netherlands;School of Biochemistry, University of New South Wales, Kensington, NSW 2033, Australia

关键词: Polypeptide;    Three-dimensional structure;    1H-NMR;    NOE;    Distance geometry;    Molecular dynamics;    AP-A;    anthopleurin-A;    NOE;    nuclear Overhauser enhancement;    NOESY;    two-dimensional nuclear Overhauser enhancement spectroscopy;    RMSD;    root mean square difference;   

DOI  :  10.1016/0014-5793(88)80931-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The solution conformation of the cardiac stimulatory sea anemone polypeptide anthopleurin-A has been characterised using distance geometry and restrained molecular dynamics calculations. A set of 253 approximate interproton distance restraints and 14 peptide backbone torsion angle restraints derived from two-dimensional ¹H-NMR spectra at 500 MHz were used as input for these calculations. 13 structures generated by either metric matrix or variable target function distance geometry calculations were refined using energy minimisation and restrained molecular dynamics. The resulting structures contain a region of twisted antiparellel β-sheet to which two separate regions of unordered chain are linked by three disulphide bonds. Two loops, one including Pro-41 and the other encompassing residues 10–18, are poorly defined by the NOE data.

【 授权许可】

Unknown