A New Efficient Method for Generating Conformations of Unfolded Proteins with Diverse Main-Chain Dihedral-Angle Distributions-Reference-Cited by-同舟云学术

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A New Efficient Method for Generating Conformations of Unfolded Proteins with Diverse Main-Chain Dihedral-Angle Distributions

Published:2011-06-27 Issue:7 Volume:7 Page:2126-2136
ISSN:1549-9618
Container-title:Journal of Chemical Theory and Computation
language:en
Short-container-title:J. Chem. Theory Comput.

Author:

Seki Yasutaka¹,Shimbo Yudai²³,Nonaka Takamasa¹,Soda Kunitsugu³

Affiliation:

1. School of Pharmacy, Iwate Medical University, Yahaba, Iwate 028-3694, Japan

2. Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata 940-2188, Japan

3. Laboratory for Computational Molecular Design, Center for Computational Life Science, RIKEN, Kobe, Hyogo 650-0047, Japan

Publisher

American Chemical Society (ACS)

Subject

Physical and Theoretical Chemistry,Computer Science Applications

Link

https://pubs.acs.org/doi/pdf/10.1021/ct100708p

Reference47 articles.

1. Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance

2. X-ray solution scattering studies of protein folding

3. The interplay between structure and function in intrinsically unstructured proteins

4. Atomic-level characterization of disordered protein ensembles

5. Biophysical characterization of intrinsically disordered proteins

Cited by 4 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. Unexpected trends in the hydrophobicity of fluorinated amino acids reflect competing changes in polarity and conformation;Physical Chemistry Chemical Physics;2019

2. Tri-peptide reference structures for the calculation of relative solvent accessible surface area in protein amino acid residues;Computational Biology and Chemistry;2015-02

3. Exploring Free-Energy Landscapes of Intrinsically Disordered Proteins at Atomic Resolution Using NMR Spectroscopy;Chemical Reviews;2014-04-11

4. A New Efficient Method for Generating Conformations of Unfolded Proteins;Seibutsu Butsuri;2012

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