Effects of the Terminal Aromatic Residues on Polyproline Conformation: Thermodynamic and Kinetic Studies
Author:
Affiliation:
1. Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan 30013, R.O.C.
2. Frontier Research Center on Fundamental and Applied Sciences of Matters, National Tsing Hua University, Hsinchu, Taiwan 30013, R.O.C.
Funder
National Science Council Taiwan
National Tsing Hua University
Ministry of Science and Technology, Taiwan
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.5b08717
Reference73 articles.
1. Creighton, T. E.Proteins: Structures and Molecular Properties.W. H. Freeman and Company:New York, 1993; p507.
2. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
3. Occurrence and role ofcis peptide bonds in protein structures
4. Aromatic–Proline Interactions: Electronically Tunable CH/π Interactions
5. Protein-protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces
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