Conformational Entropy from Slowly Relaxing Local Structure Analysis of 15N–H Relaxation in Proteins: Application to Pheromone Binding to MUP-I in the 283–308 K Temperature Range-Reference-Cited by-同舟云学术

Conformational Entropy from Slowly Relaxing Local Structure Analysis of 15N–H Relaxation in Proteins: Application to Pheromone Binding to MUP-I in the 283–308 K Temperature Range

Published:2017-09-08 Issue:37 Volume:121 Page:8684-8692
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Žídek Lukáš¹²,Meirovitch Eva³^ORCID

Affiliation:

1. Central European Institute of Technology, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic

2. National Center for Biomolecular Research, Faculty of Science, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic

3. The Mina and Everard Goodman Faculty of Life Sciences, Bar-Ilan University, Ramat-Gan 52900, Israel

Funder

Israel Science Foundation

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.7b06049

Reference46 articles.

1. NMR order parameters and free energy: an analytical approach and its application to cooperative calcium(2+) binding by calbindin D9k

2. Insights into the local residual entropy of proteins provided by NMR relaxation

3. Contributions to Conformational Entropy Arising from Bond Vector Fluctuations Measured from NMR-Derived Order Parameters: Application to Protein Folding

4. The role of backbone conformational heat capacity in protein stability: Temperature dependent dynamics of the B1 domain ofStreptococcalprotein G

5. Backbone dynamics of proteins as studied by nitrogen-15 inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

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