Cooperative Cold Denaturation: The Case of the C-Terminal Domain of Ribosomal Protein L9-Reference-Cited by-同舟云学术

Cooperative Cold Denaturation: The Case of the C-Terminal Domain of Ribosomal Protein L9

Published:2013-03-26 Issue:14 Volume:52 Page:2402-2409
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Luan Bowu¹,Shan Bing¹,Baiz Carlos²,Tokmakoff Andrei²,Raleigh Daniel P.¹³

Affiliation:

1. Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, United States

2. Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States

3. Graduate Program in Biochemistry and Structural Biology and Graduate Program in Biophysics, Stony Brook University, Stony Brook, New York 11794-3400, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi3016789

Reference40 articles.

1. On the molecular origin of cold denaturation of globular proteins

2. Hydrophobicity at low temperatures and cold denaturation of a protein

3. Unifying Microscopic Mechanism for Pressure and Cold Denaturations of Proteins

4. Microscopic Mechanism for Cold Denaturation

5. Protein Cold Denaturation as Seen From the Solvent

Cited by 31 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Key Factors Controlling Fibril Formation of Proteins;Acta Physica Polonica A;2024-03

2. Temperature effects on hydrophobic interactions: Implications for protein unfolding;Chemical Physics;2022-07

3. CalFitter 2.0: Leveraging the power of singular value decomposition to analyse protein thermostability;Nucleic Acids Research;2022-05-17

4. Recipes for Inducing Cold Denaturation in an Otherwise Stable Protein;Journal of the American Chemical Society;2022-04-15

5. From Protein Design to the Energy Landscape of a Cold Unfolding Protein;The Journal of Physical Chemistry B;2022-02-07