Simulation of the highly stable protein: bovine γb-crystallin at room and high temperature

Title:Simulation of the highly stable protein: bovine γb-crystallin at room and high temperature

Volume: 7 Issue: 4

Author(s): Andrew G. Purkiss, Christine Slingsby and Julia M. Goodfellow*

Affiliation:

• Department of Crystallography, Birkbeck College, University of London, Malet Street, London, WCIE 7HX, UK

Abstract: The behavior of the eye-lens protein bovine γB-crystallin is investigated at both room temperature and at an elevated temperature (at which unfolding would be expected to occur) using molecular dynamics. Even in the high temperature simulation, there is little loss ·of secondary structure. Although only small changes in the tertiary contacts occur, even at high temperature, fluctuations in conformation are much more pronounced at 500K than 300K. These results agree with the experimental observations on the remarkable stability of the eye lens proteins and also indicate where the initial events in unfolding are occurring.

Cite this article as:

Purkiss G. Andrew, Slingsby Christine and Goodfellow M. Julia*, Simulation of the highly stable protein: bovine γb-crystallin at room and high temperature, Protein & Peptide Letters 2000; 7 (4) . https://dx.doi.org/10.2174/092986650704221206152154

DOI https://dx.doi.org/10.2174/092986650704221206152154	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305