Molecular Origin of Constant m-Values, Denatured State Collapse, and Residue-Dependent Transition Midpoints in Globular Proteins-Reference-Cited by-同舟云学术

Molecular Origin of Constant m-Values, Denatured State Collapse, and Residue-Dependent Transition Midpoints in Globular Proteins

Published:2009-04-13 Issue:17 Volume:48 Page:3743-3754
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

O’Brien Edward P.¹,Brooks Bernard R.¹,Thirumalai D.¹

Affiliation:

1. Biophysics Program, Institute for Physical Science and Technology, and Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, and Laboratory of Computational Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8021119

Reference65 articles.

1. How do small single-domain proteins fold?

2. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range

3. Urea and Guanidine Hydrochloride Denaturation of Ribonuclease, Lysozyme, α-Chymotrypsin, and b-Lactoglobulin

4. [14]Determination and analysis of urea and guanidine hydrochloride denaturation curves

5. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl .alpha.-chymotrypsin using different denaturants

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