Study of Pair Contact Formation among Hydrophobic Residues in a Model HP-36 Protein: Relationship between Contact Order Parameter and Rate of Folding and Collapse-Reference-Cited by-同舟云学术

Study of Pair Contact Formation among Hydrophobic Residues in a Model HP-36 Protein: Relationship between Contact Order Parameter and Rate of Folding and Collapse

Published:2003-10-01 Issue:42 Volume:107 Page:11768-11773
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Srinivas Goundla¹,Bagchi Biman¹

Affiliation:

1. Solid State and Structural Chemistry Unit, Indian Institute of Science, Bangalore, India 560 012

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/jp022333j

Reference28 articles.

1. Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures

2. First-Order Disorder-to-Order Transition in an Isolated Homopolymer Model

3. A metastable state in folding simulations of a protein model

4. Variational Theory for Site Resolved Protein Folding Free Energy Surfaces

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