Force-Induced Insulin Dimer Dissociation: A Molecular Dynamics Study-Reference-Cited by-同舟云学术

Force-Induced Insulin Dimer Dissociation: A Molecular Dynamics Study

Published:2006-04-01 Issue:16 Volume:128 Page:5330-5331
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kim Taeho¹,Rhee Alexander¹,Yip Christopher M.¹

Affiliation:

1. Chemical Engineering & Applied Chemistry, Institute of Biomaterials & Biomedical Engineering, and The Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, 160 College Street, Toronto, ON, Canada M5S 3E1

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0607382

Reference17 articles.

1. Three-dimensional solution structure of an insulin dimer

2. The solution structure of a monomeric insulin. A two-dimensional 1H-NMR study of des-(B26-B30)-insulin in combination with distance geometry and restrained molecular dynamics

3. NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain

4. A Comparison of the Dynamic Behavior of Monomeric and Dimeric Insulin Shows Structural Rearrangements in the Active Monomer

5. YY1 is an initiator sequence-binding protein that directs and activates transcription in vitro

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