Probing the functional conformations of an atypical proline-rich fusion peptide
Author:
Affiliation:
1. Department of Biophysics
2. Molecular Biology and Bioinformatics
3. University of Calcutta
4. Kolkata 700009
5. India
Abstract
Simulations confirm a propensity for extended and solvent exposed conformations of the p15 fusion peptide capable of membrane targeting.
Funder
Council of Scientific and Industrial Research, India
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP02216C
Reference72 articles.
1. Cell-Cell Membrane Fusion Induced by p15 Fusion-associated Small Transmembrane (FAST) Protein Requires a Novel Fusion Peptide Motif Containing a Myristoylated Polyproline Type II Helix
2. Structure of Poly-L-Proline
3. A survey of left-handed polyproline II helices
4. Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
5. The Structure of Fibrous Proteins of the Collagen-Gelatin Group
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