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A fragment of staphylococcal nuclease with an OB‐fold structure shows hydrogen‐exchange protection factors in the range reported for “molten globules”
Author(s) -
Alexandrescu Andrei T.,
Dames Sonja A.,
Wiltscheck Ronald
Publication year - 1996
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560050924
Subject(s) - chemistry , molten globule , solvent , nuclease , crystallography , hydrogen , protein structure , enzyme , biochemistry , organic chemistry
Hydrogen‐exchange rates for an OB‐fold subdomain fragment of staphylococcal nuclease have been measured at pH 4.7 and 4 °C, conditions close to the minimum of acid/base catalyzed exchange. The strongest protection from solvent exchange is observed for residues from a five‐stranded β‐barrel in the NMR structure of the protein. Protection factors, calculated from the experimental hydrogen‐exchange rates, range between 1 and 190. Similarly small protection factors have in many cases been attributed to “molten globule” conformations that are supposed to lack a specific tertiary structure. The present results suggest that marginal protection from solvent exchange does not exclude well‐defined structure.