Milieu-Initiated Inversion of the Aqueous Polyproline II/β Propensity in the Alanine Tripeptide: Aggregation Origin of the Onset of Amyloid Formation-Reference-Cited by-同舟云学术

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Milieu-Initiated Inversion of the Aqueous Polyproline II/β Propensity in the Alanine Tripeptide: Aggregation Origin of the Onset of Amyloid Formation

Published:2018-04-04 Issue:16 Volume:122 Page:4428-4432
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Mirkin Noemi G.¹,Krimm Samuel¹^ORCID

Affiliation:

1. LSA Biophysics, University of Michigan, 930 N. University Avenue, Ann Arbor, Michigan 48109, United States

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/acs.jpcb.8b00612

Reference35 articles.

1. New chain conformations of poly(glutamic acid) and polylysine

2. The Circular Dichroism Spectrum and Structure of Unordered Polypeptides and Proteins

3. Water interaction differences determine the relative energetic stability of the polyproline II conformation of the alanine dipeptide in aqueous environments

4. Other species in the aqueous environment of a peptide can invert its intrinsic solvated polyproline II/beta propensity: Implications for amyloid formation

Cited by 1 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. Hydrogen sulfide concentration in the milieu of the hydrated alanine dipeptide determines its polyproline II‐beta propensity: Main chain contribution to the energetic origin of the formation of amyloid;Biopolymers;2020-05-07

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