Skip to content
Licensed Unlicensed Requires Authentication Published by De Gruyter November 27, 2014

Some insights into the transition state ensemble of the folding of globular proteins

  • Jacques Chomilier EMAIL logo

Corresponding author: Jacques Chomilier, Guest Editor, UPMC, IMPMC, 4 Place Jussieu, 75251 Paris, France, E-mail:

References

1. Ittah V, Haas E. Nonlocal interactions stabilize long range loops in the initial folding intermediates of reduced bovine pancreatic trypsin inhibitor. Biochemistry 1995;34:4493–506.10.1021/bi00013a042Search in Google Scholar PubMed

2. Orevi T, Rahamin G, Shemesh S, Ben Ishai E, Amir D, Haas E. Fast closure of long loops at the initiation of the folding transition of globular proteins studied by time resolved FRET-based methods. Bio-Algorithms Med-Syst 2014;10.10.1515/bams-2014-0018Search in Google Scholar

3. Bonet J, Fiser A, Oliva B, Fernandez-Fuentes N. Smotifs as structural local descriptors of super-secondary elements: classification, completeness, and applications. Bio-Algorithms Med-Syst 2014;10.10.1515/bams-2014-0016Search in Google Scholar

4. Das R, Baker D. Macromolecular modeling with Rosetta. Annu Rev Biochem 2008;77:363–82.10.1146/annurev.biochem.77.062906.171838Search in Google Scholar PubMed

5. Lau K, Dill K. A lattice statistical mechanics model of the conformational and sequence spaces of proteins. Macromolecules 1989;22:3986–97.10.1021/ma00200a030Search in Google Scholar

6. Mann M, Backofen R. Exact methods for lattice protein models. Bio-Algorithms Med-Syst 2014;10.10.1515/bams-2014-0014Search in Google Scholar

7. Acuna R, Lacroix Z, Papandreou N, Chomilier J. Prediction of the protein folding nucleus with most interacting residues. Bio-Algorithms Med-Syst 2014;10.10.1515/bams-2014-0015Search in Google Scholar

8. Techner S, Kosciolek T, Jones D. Opportunities and limitations in applying coevolution-derived contacts to protein structure prediction. Bio-Algorithms Med-Syst 2014;10.10.1515/bams-2014-0013Search in Google Scholar

9. Weigt M, White R, Szurmant H, Hoch J, Hwa T. Identification of direct residue contacts in protein-protein interaction by message passing. Proc Natl Acad Sci USA 2009;106:67–72.10.1073/pnas.0805923106Search in Google Scholar PubMed PubMed Central

10. Cruzeiro L. A kinetic mechanism for in vivo protein folding. Bio-Algorithms Med-Syst 2014;10:117–29.10.1515/bams-2014-0010Search in Google Scholar

Published Online: 2014-11-27
Published in Print: 2014-12-19

©2014 by De Gruyter

Downloaded on 25.4.2024 from https://www.degruyter.com/document/doi/10.1515/bams-2014-0020/html
Scroll to top button