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Multiple subsets of side-chain packing in partially folded states of a-lactalbumins
journal contribution
posted on 2023-06-07, 23:36 authored by K. Hun Mok, Toshio Nagashima, Iain Day, P J Hore, Christopher M DobsonPhotochemically induced dynamic nuclear polarization NMR pulse- labeling techniques have been used to obtain detailed information about side-chain surface accessibilities in the partially folded (mol- ten globule) states of bovine and human -lactalbumin prepared under a variety of well defined conditions. Pulse labeling involves generating nuclear polarization in the partially folded state, rap- idly refolding the protein within the NMR sample tube, then detecting the polarization in the well dispersed native-state spec- trum. Differences in the solvent accessibility of specific side chains in the various molten globule states indicate that the hydrophobic clusters involved in stabilizing the -lactalbumin fold can be formed from interactions between a variety of different hydro- phobic residues in both native and nonnative environments. The multiple subsets of hydrophobic clusters are likely to result from the existence of distinct but closely related local minima on the free-energy landscape of the protein and show that the fold and topology of a given protein may be formed from degenerate groups of side chains.
History
Publication status
- Published
Journal
Proceedings of the National Academy of SciencesISSN
0027-8424Publisher
National Academy of SciencesPublisher URL
External DOI
Issue
25Volume
102Page range
8899-8904Pages
6.0Department affiliated with
- Chemistry Publications
Notes
ID contributed to the acquisition, analysis and interpretation of the data and co authored the paper. First demonstration of the side-chain packing heterogeneity in alpha-lactalbumin molten globules on a residue-specific basis, also provides a clear demonstration of the applicability of the injection device developed previously.Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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