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Article

Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy.

Proceedings of the National Academy of Sciences of the United States of America - 18 Jan 1994

Jacobs M D, Fox R O

Abstract excerpt

Pulsed hydrogen-deuterium exchange during refolding was used to probe the protection of backbone amide hydrogens from solvent exchange of the staphylococcal nuclease Pro117-->Gly variant. The extent of exchange for 39 residues was determined by two-dimensional proton NMR after refolding for 5 ms to 10 s. Three kinetic phases are inferred. Modest protection of amides in the early refolding intermediate composed of...

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Identifiers

PMID: 8290547
DOI: 10.1073/pnas.91.2.449
PMCID: PMC42966

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