期刊论文详细信息
FEBS Letters | |
Low‐temperature 1H‐NMR evidence of the folding of isolated ribonuclease S‐peptide | |
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
【 预 览 】
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