Molecular Insight into the High Thermal Stability of Metalloprotein Azurin-Reference-Cited by-同舟云学术

Molecular Insight into the High Thermal Stability of Metalloprotein Azurin

Published:2022-03-24 Issue:13 Volume:126 Page:2496-2506
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Joy Albin¹^ORCID,Biswas Rajib²^ORCID

Affiliation:

1. Department of Chemistry, Indian Institute of Technology Tirupati, Yerpedu 517619, Andhra Pradesh, India

2. Department of Chemistry and Center for Atomic, Molecular and Optical Sciences & Technologies, Indian Institute of Technology Tirupati, Yerpedu 517619, Andhra Pradesh, India

Funder

Indian Institute of Technology Tirupati

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.2c00622

Reference89 articles.

1. Modelling protein unfolding: hen egg-white lysozyme

2. Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol

3. Eftink, M.; Pedigo, S. In Encyclopedia of Physical Science and Technology, 3rd ed. Meyers, R. A., Ed. Academic Press: New York, 2003; pp 179–190.

4. Chapter 1 Practical Approaches to Protein Folding and Assembly

5. Computational and Theoretical Methods for Protein Folding

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1. Significance of the Disulfide Bridge in the Structure and Stability of Metalloprotein Azurin;The Journal of Physical Chemistry B;2024-01-18

2. Role of Metal Cofactor in Enhanced Thermal Stability of Azurin;The Journal of Physical Chemistry B;2023-05-15