Conformational Folding and Stability of the HET-C2 Glycolipid Transfer Protein Fold: Does a Molten Globule-like State Regulate Activity?-Reference-Cited by-同舟云学术

Conformational Folding and Stability of the HET-C2 Glycolipid Transfer Protein Fold: Does a Molten Globule-like State Regulate Activity?

Published:2011-05-19 Issue:23 Volume:50 Page:5163-5171
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kenoth Roopa¹,Kamlekar Ravi Kanth¹,Simanshu Dhirendra K.²,Gao Yongguang¹,Malinina Lucy³,Prendergast Franklyn G.⁴,Molotkovsky Julian G.⁵,Patel Dinshaw J.²,Venyaminov Sergei Y.⁴,Brown Rhoderick E.¹

Affiliation:

1. The Hormel Institute, University of Minnesota, Austin, Minnesota 55912, United States

2. Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, United States

3. Structural Biology, CIC bioGUNE, Derio, Spain

4. Mayo Clinic College of Medicine, Rochester, Minnesota 55905, United States

5. Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200382c

Reference64 articles.

1. α-lactalbumin: compact state with fluctuating tertiary structure?

2. Unfolded proteins, compact states and molten globules

3. Protein Folding: Solid evidence for molten globules

4. Kinetic and equilibrium folding intermediates

5. Interaction of Diphtheria Toxin T Domain with Molten Globule-Like Proteins and Its Implications for Translocation

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