For the Sequence YKGQ, the Turn and Extended Conformational Forms Are Separated by Small Barriers and the Turn Propensity Persists Even at High Temperatures: Implications for Protein Folding-Reference-Cited by-同舟云学术

For the Sequence YKGQ, the Turn and Extended Conformational Forms Are Separated by Small Barriers and the Turn Propensity Persists Even at High Temperatures: Implications for Protein Folding

Published:2012-03-16 Issue:12 Volume:116 Page:3850-3860
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Kaur Harpreet¹,Sasidhar Yellamraju U.¹

Affiliation:

1. Department of Chemistry, Indian Institute of Technology Bombay, Powai, Mumbai 400 076, India

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/jp210227s

Reference75 articles.

1. The crystal structure of the ternary complex of staphylococcal nuclease, Ca2+ and the inhibitor pdTp, refined at 1.65 Å

2. Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy.

3. Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange

4. β-Hairpins with native-like and non-native hydrogen bonding patterns could form during the refolding of staphylococcal nuclease

5. Loop propensity of the sequence YKGQP from staphylococcal nuclease: implications for the folding of nuclease

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