Physical origins of the high structural stability of CLN025 with only ten residues
Author:
Affiliation:
1. Institute of Advanced Energy, Kyoto University, Uji, Kyoto 611-0011, Japan
Funder
JSPS (Japan Society for the Promotion of Science) Grant-in-Aid for Scientific Research (B)
Publisher
AIP Publishing
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://aip.scitation.org/doi/pdf/10.1063/1.4894753
Reference58 articles.
1. Protein folding and misfolding
2. 10 Residue Folded Peptide Designed by Segment Statistics
3. Crystal Structure of a Ten-Amino Acid Protein
4. Molecular Dynamics Analysis of the Conformations of a β-Hairpin Miniprotein
5. The CLN025 Decapeptide Retains a β-Hairpin Conformation in Urea and Guanidinium Chloride
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