Transition Dipoles from 1D and 2D Infrared Spectroscopy Help Reveal the Secondary Structures of Proteins: Application to Amyloids
Author:
Affiliation:
1. Department of Chemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706-1396, United States
Funder
National Institute of Diabetes and Digestive and Kidney Diseases
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.5b07706
Reference62 articles.
1. Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution
2. Two-dimensional Infrared Spectroscopy Provides Evidence of an Intermediate in the Membrane-catalyzed Assembly of Diabetic Amyloid
3. Attenuated total reflection IR spectroscopy as a tool to investigate the structure, orientation and tertiary structure changes in peptides and membrane proteins
4. Applications of 2D IR Spectroscopy to Peptides, Proteins, and Hydrogen-Bond Dynamics
5. Frequency Distribution of the Amide-I Vibration Sorted by Residues in Amyloid Fibrils Revealed by 2D-IR Measurements and Simulations
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