Multiple subsets of side-chain packing in partially folded states of α-lactalbumins

Mok, K. Hun, Nagashima, Toshio, Day, Iain J, Hore, P J and Dobson, Christopher M (2005) Multiple subsets of side-chain packing in partially folded states of α-lactalbumins. Proceedings of the National Academy of Sciences, 102 (25). pp. 8899-8904. ISSN 0027-8424

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Abstract

Photochemically 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.

Item Type: Article
Additional Information: 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.
Schools and Departments: School of Life Sciences > Chemistry
Depositing User: Iain Day
Date Deposited: 06 Feb 2012 19:38
Last Modified: 21 May 2012 15:47
URI: http://sro.sussex.ac.uk/id/eprint/21598
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