A fragment of staphylococcal nuclease with an OB‐fold structure shows hydrogen‐exchange protection factors in the range reported for “molten globules”

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 NM...

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Bibliographic Details
Published in:Protein science 1996-09, Vol.5 (9), p.1942-1946
Main Authors: Alexandrescu, Andrei T., Dames, Sonja A., Wiltscheck, Ronald
Format: Article
Language:English
Subjects:
Hydrogen Bonding
hydrogen exchange
Hydrogen-Ion Concentration
kinetic intermediate
Kinetics
Magnetic Resonance Spectroscopy
Micrococcal Nuclease - chemistry
Models, Molecular
molten globule
NMR structure
Peptide Fragments - chemistry
protection factors
Protein Folding
Protein Structure, Secondary
Temperature
Thermodynamics
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Summary: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.
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560050924