Reference : The Folding Process of Hen Lysozyme: A Perspective from the 'New View'
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/16641
The Folding Process of Hen Lysozyme: A Perspective from the 'New View'
English
Matagne, André mailto [University of Oxford > Oxford Centre for Molecular Sciences > > >]
Dobson, Christopher M. [University of Oxford > Oxford Centre for Molecular Sciences > > >]
Apr-1998
Cellular and Molecular Life Sciences : CMLS
54
4
363-71
Yes (verified by ORBi)
International
1420-682X
[en] protein folding ; hen egg white lysozyme ; biophysical methods ; kinetic partitioning ; folding intermediates ; folding domains ; nonnative interactions ; energy surface
[en] How a conformationally disordered polypeptide chain rapidly and efficiently achieves its well-defined native structure is still a major question in modern structural biology. Although much progress has been made towards rationalizing the principles of protein structure and dynamics, the mechanism of the folding process and the determinants of the final fold are not yet known in any detail. One protein for which folding has been studied in great detail by a combination of diverse techniques is hen lysozyme. In this article we review the present state of our knowledge of the folding process of this enzyme and focus in particular on recent experiments to probe some of its specific features. These results are then discussed in the context of the 'new view' of protein folding based on energy surfaces and landscapes. It is shown that a schematic energy surface for lysozyme folding, which is broadly consistent with our experimental data, begins to provide a unified model for protein folding through which experimental and theoretical ideas can be brought together.
http://hdl.handle.net/2268/16641

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Open access
Matagne&DobsonCMLS.pdfNo commentaryPublisher postprint3.3 MBView/Open

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.