Remodeling of the Folding Free Energy Landscape of Staphylococcal Nuclease by Cavity-Creating Mutations-Reference-Cited by-同舟云学术

Remodeling of the Folding Free Energy Landscape of Staphylococcal Nuclease by Cavity-Creating Mutations

Published:2012-11-13 Issue:47 Volume:51 Page:9535-9546
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Roche Julien¹,Dellarole Mariano¹,Caro Jose A.²,Guca Ewelina¹,Norberto Douglas R.³,Yang Yinshan¹,Garcia Angel E.⁴,Roumestand Christian¹,García-Moreno Bertrand²,Royer Catherine A.¹

Affiliation:

1. Centre de Biochimie Structurale, INSERM U554, CNRS UMR 5048, Universités de Montpellier, Montpellier, France

2. Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, United States

3. Department of Biochemistry, Institute of Biology, University of Campinas, Campinas, Brazil

4. Department of Physics and Applied Physics and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301071z

Reference71 articles.

1. An Experimental Approach to the Study of the Folding of Staphylococcal Nuclease

2. Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction

3. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.

4. The Foldon Substructure of Staphylococcal Nuclease

5. Early Events During Folding of Wild-type Staphylococcal Nuclease and a Single-tryptophan Variant Studied by Ultrarapid Mixing

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