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Low‐temperature 1 H‐NMR evidence of the folding of isolated ribonuclease S‐peptide
Author(s) -
Rico M.,
Nieto J.L.,
Santoro J.,
Bermejo F.J.,
Herranz J.,
Gallego E.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80779-0
Subject(s) - ribonuclease , chemistry , peptide , crystallography , folding (dsp implementation) , helix (gastropod) , molecule , chemical shift , ribonuclease t1 , proton nmr , protein folding , stereochemistry , rnase p , rna , biochemistry , biology , organic chemistry , ecology , snail , electrical engineering , gene , engineering
The temperature (−7°C to 45°C, pH 5.4) and pH (0°C) dependence of 1 H 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 1 H‐NMR at low temperature for the isolated S‐peptide are compatible with the structure shown by the same molecule in the ribonuclease S crystal.