Aromatic Residues Engineered into the β-Turn Nucleation Site of Ubiquitin Lead to a Complex Folding Landscape, Non-Native Side-Chain Interactions, and Kinetic Traps-Reference-Cited by-同舟云学术

Aromatic Residues Engineered into the β-Turn Nucleation Site of Ubiquitin Lead to a Complex Folding Landscape, Non-Native Side-Chain Interactions, and Kinetic Traps

Published:2008-11-08 Issue:48 Volume:47 Page:12910-12922
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rea Anita M.¹,Simpson Emma R.¹,Meldrum Jill K.¹,Williams Huw E. L.¹,Searle Mark S.¹

Affiliation:

1. Centre for Biomolecular Sciences,School of Chemistry, University Park, Nottingham NG7 2RD, U.K.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi801330r

Reference50 articles.

1. How do small single-domain proteins fold?

2. NMR Analysis of the Conformational Properties of the Trapped on-pathway Folding Intermediate of the Bacterial Immunity Protein Im7

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4. Evidence for Sequential Barriers and Obligatory Intermediates in Apparent Two-state Protein Folding

5. Folding Kinetics of Staphylococcal Nuclease Studied by Tryptophan Engineering and Rapid Mixing Methods

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