Molecular Dynamics of a 15-Residue Poly(l-alanine) in Water: Helix Formation and Energetics-Reference-Cited by-同舟云学术

Molecular Dynamics of a 15-Residue Poly(l-alanine) in Water: Helix Formation and Energetics

Published:1999-01-14 Issue:4 Volume:121 Page:605-612
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Takano Mitsunori¹,Yamato Takahisa¹,Higo Junichi¹,Suyama Akira¹,Nagayama Kuniaki¹

Affiliation:

1. Contribution from the Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, 3-8-1, Komaba, Meguro-ku, Tokyo 153-8902, Japan, Department of Physics, Graduate School of Science, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8602, Japan, Biomolecular Engineering Research Institute, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan, and National Institute for Physiological Sciences, Myodaiji, Okazaki 444-8585, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja982919c

Reference66 articles.

1. Direct observation of fast protein folding: the initial collapse of apomyoglobin.

2. Fast events in protein folding: Relaxation dynamics of secondary and tertiary structure in native apomyoglobin

3. Fast Events in Protein Folding: Relaxation Dynamics and Structure of the I Form of Apomyoglobin

4. The core of apomyoglobin E-form folds at the diffusion limit

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