Probing secondary structures of end-capped tripeptide, BOC–Phe–Aib–Leu–OMe by combined study of infrared spectroscopy and quantum chemistry calculation
Author:
Publisher
Elsevier BV
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Reference33 articles.
1. A backbone-based theory of protein folding
2. Competition between local conformational preferences and secondary structures in gas-phase model tripeptides as revealed by laser spectroscopy and theoretical chemistry
3. Characterization of the Conformational Probability of N-Acetyl-Phenylalanyl-NH2 by RHF, DFT, and MP2 Computation and AIM Analyses, Confirmed by Jet-Cooled Infrared Data
4. The Gas-Phase Dipeptide Analogue Acetyl-phenylalanyl-amide: A Model for the Study of Side Chain/Backbone Interactions in Proteins
5. Intrinsic Folding of Small Peptide Chains: Spectroscopic Evidence for the Formation of β-Turns in the Gas Phase
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1. Electropolymerization of some amino acids on platinum electrode;Bionatura;2023-06-15
2. Limitations of Spectral Subtraction in the Elimination of Infrared Water Vapor Bands;SPECTROSC SPECT ANAL;2017
3. The structure and IR signatures of the arginine-glutamate salt bridge. Insights from the classical MD simulations;The Journal of Chemical Physics;2015-06-07
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