Isotope-edited vibrational circular dichroism study reveals a flexible N-terminal structure of islet amyloid peptide (NFGAIL) in amyloid fibril form: A site-specific local structural analysis
Author:
Funder
Central Leather Research Institute
Science and Engineering Research Board
Publisher
Elsevier BV
Subject
Structural Biology
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1. Structural Insights into the Amyloid Fibril Polymorphism Using an Isotope-Edited Vibrational Circular Dichroism Study at the Amino Acid Residue Level;The Journal of Physical Chemistry B;2023-09-05
2. π‐System Functionalization Transforms Amyloidogenic Peptide Fragment of Human Islet Amyloid Polypeptide into a Super Hydrogelator;Chemistry – An Asian Journal;2023-01-11
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