The ubiquitous buried water in the beta‐trefoil architecture contributes to the folding nucleus and ~20% of the folding enthalpy
Author:
Affiliation:
1. Department of Biomedical Sciences Florida State University Tallahassee Florida USA
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4192
Reference42 articles.
1. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
2. Water-Inserted α-Helical Segments Implicate Reverse Turns as Folding Intermediates
3. The turn sequence directs β- strand alignment in designed β-hairpins
4. Three key residues form a critical contact network in a protein folding transition state
5. Identification of a Key Structural Element for Protein Folding Within β-Hairpin Turns
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