Folding Studies of a Linear Pentamer Peptide Adopting a Reverse Turn Conformation in Aqueous Solution through Molecular Dynamics Simulation-Reference-Cited by-同舟云学术

Folding Studies of a Linear Pentamer Peptide Adopting a Reverse Turn Conformation in Aqueous Solution through Molecular Dynamics Simulation

Published:2000-07-28 Issue:33 Volume:104 Page:8023-8034
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Wu Xiongwu¹,Wang Shaomeng¹

Affiliation:

1. Georgetown Institute for Cognitive and Computational Sciences and Lombardi Cancer Center and Departments of Oncology and Neuroscience, Georgetown University Medical Center, Research Building, WP05, 3970 Reservoir Road, Washington, DC 20007

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp000529i

Reference49 articles.

1. Folding of immunogenic peptide fragments of proteins in water solution

2. NMR evidence of a short linear peptide that folds into a .beta.-hairpin in aqueous solution

3. NMR Solution Structure of the Isolated N-Terminal Fragment of Protein-G B1 Domain. Evidence of Trifluoroethanol Induced Native-Like .beta.-Hairpin Formation

4. Folding dynamics and mechanism of β-hairpin formation

5. Nanosecond timescale folding dynamics of a pentapeptide in water

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