Extensive Formation of Off-Pathway Species during Folding of an α−β Parallel Protein Is Due to Docking of (Non)native Structure Elements in Unfolded Molecules-Reference-Cited by-同舟云学术

Extensive Formation of Off-Pathway Species during Folding of an α−β Parallel Protein Is Due to Docking of (Non)native Structure Elements in Unfolded Molecules

Published:2008-11-19 Issue:50 Volume:130 Page:16914-16920
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Nabuurs Sanne M.¹,Westphal Adrie H.¹,van Mierlo Carlo P. M.¹

Affiliation:

1. Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja803841n

Reference51 articles.

1. Understanding protein folding via free-energy surfaces from theory and experiment

2. Protein Folding and Unfolding at Atomic Resolution

3. Three key residues form a critical contact network in a protein folding transition state

4. Funnels, pathways, and the energy landscape of protein folding: A synthesis

5. Random-coil behavior and the dimensions of chemically unfolded proteins

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