A theoretical study of the stability of disulfide bridges in various β-sheet structures of protein segment models-Reference-Cited by-同舟云学术

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A theoretical study of the stability of disulfide bridges in various β-sheet structures of protein segment models

Published:2014-02 Issue: Volume:593 Page:48-54
ISSN:0009-2614
Container-title:Chemical Physics Letters
language:en
Short-container-title:Chemical Physics Letters

Author:

Galant Natalie J.,Song Heeyeon Cheryl,Jákli Imre,Viskolcz Bela,Csizmadia Imre G.,Knak Jensen Svend J.,Perczel Andras

Publisher

Elsevier BV

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Reference32 articles.

1. Protein aggregation and neurodegenerative disease

2. The Amyloid State of Proteins in Human Diseases

3. Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen

4. Structure of the cross-β spine of amyloid-like fibrils

5. Dead-End Street of Protein Folding: Thermodynamic Rationale of Amyloid Fibril Formation

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. Design and Synthesis of Cross-Link-Dense Peptides by Manipulating Regioselective Bisthioether Cross-Linking and Orthogonal Disulfide Pairing;The Journal of Organic Chemistry;2019-03-21

2. Modulating amyloid fibrillation in a minimalist model peptide by intermolecular disulfide chemical reduction;Physical Chemistry Chemical Physics;2019

3. Effect of Anions on Nanofiber Formation of β-sheet Propensity Amphiphile Peptide;IOP Conference Series: Materials Science and Engineering;2018-05

4. Quantum Chemical Calculations on Small Protein Models;Protein Modelling;2014

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