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Rapid formation of non-native contacts during the folding of HPr revealed by real-time photo-CIDNP NMR and stopped-flow fluorescence experiments.

Abstract:

We report the combined use of real-time photo-CIDNP NMR and stopped-flow fluorescence techniques to study the kinetic refolding of a set of mutants of a small globular protein, HPr, in which each of the four phenylalanine residues has in turn been replaced by a tryptophan residue. The results indicate that after refolding is initiated, the protein collapses around at least three, and possibly all four, of the side-chains of these residues, as (i) the observation of transient histidine photo-C...

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Publication status:
Published

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Journal:
Journal of molecular biology
Volume:
330
Issue:
2
Pages:
397-407
Publication date:
2003-07-01
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
Source identifiers:
32394

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