Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptide

FEBS Letters

Herranz, J.¹  Santoro, J.¹  Rico, M.¹  Gallego, E.¹  Nieto, J.L.¹  Bermejo, F.J.¹ 

[1] Instituto de Estructura de la Materia, CSIC, Serrano 119, Madrid-6, Spain

关键词: 1H-NMR;    Ribonuclease S-peptide;    Peptide folding;    Helical structure;    Sidechain interaction;    CD;    circular dichroism;    NMR;    nuclear magnetic resonance;    TSP;    sodium 2;    2;    3;    3-tetradeutero-3-trimethylsilylpropionate;    abbreviations for the amino acids;    are those recommended by the IUPAC—IUB commission on biochemical nomenclature;    Im;    imidazole;    Gnd;    guanidino;   

DOI  :  10.1016/0014-5793(83)80779-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The temperature (−7°C to 45°C, pH 5.4) and pH (0°C) dependence of ¹H chemical shifts of ribonuclease S-peptide (5 mM, 1 M NaCl) has been measured at 360 MHz. The observed variations evidence the formation of a partial helical structure, involving the fragment Thr-3—Met-13. Two salt-bridges stabilize the helix: those formed by Glu-9⁻…His-12⁺ and Glu-2⁻…Arg-10⁺. The structural features deduced from the ¹H-NMR at low temperature for the isolated S-peptide are compatible with the structure shown by the same molecule in the ribonuclease S crystal.

【 授权许可】

Unknown