Racemic Peptides from Amyloid β and Amylin Form Rippled β-Sheets Rather Than Pleated β-Sheets
Author:
Affiliation:
1. Dept. of Chemistry and Biochemistry, UCSC, 1156 High Street, Santa Cruz, California 95064, United States
2. Dept. of Chemistry and Biochemistry, UCLA, 607 Charles E. Young Drive East, Box 951569, Los Angeles, California 90095-1569, United States
Funder
Division of Molecular and Cellular Biosciences
California NanoSystems Institute
National Institute on Aging
U.S. Department of Energy
Seaver Institute
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.3c11712
Reference40 articles.
1. Using chirality to probe the conformational dynamics and assembly of intrinsically disordered amyloid proteins
2. Exploiting the Right Side of the Ramachandran Plot: Substitution of Glycines by d-Alanine Can Significantly Increase Protein Stability
3. Using D-amino acids to delineate the mechanism of protein folding: Application to Trp-cage
4. Toward the Active Conformation of Insulin
5. Suppression of Oligomer Formation and Formation of Non‐Toxic Fibrils upon Addition of Mirror‐Image Aβ42 to the Natural l ‐Enantiomer
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