Comment on “Microhydration of Biomolecules: Revealing the Native Structures by Cold Ion IR Spectroscopy”
Author:
Affiliation:
1. Department of Chemistry, University of Wisconsin─Madison, 1101 University Avenue, Madison, Wisconsin 53706, United States
Funder
Wisconsin Alumni Research Foundation
Basic Energy Sciences
Division of Graduate Education
Publisher
American Chemical Society (ACS)
Subject
General Materials Science,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.1c02211
Reference24 articles.
1. Microhydration of Biomolecules: Revealing the Native Structures by Cold Ion IR Spectroscopy
2. Competition between Solvation and Intramolecular Hydrogen-Bonding in Microsolvated Protonated Glycine and β-Alanine
3. Microsolvation Structures of Protonated Glycine and l-Alanine
4. Probing Solvation-Induced Structural Changes in Conformationally Flexible Peptides: IR Spectroscopy of Gly3H+·(H2O)
5. Revealing the structure of isolated peptides: IR-IR predissociation spectroscopy of protonated triglycine isomers
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4. Effects of Methyl Side Chains on the Microsolvation Structure of Protonated Tripeptides;The Journal of Physical Chemistry A;2023-07-21
5. Revealing the Structure of Tryptophan in Microhydrated Complexes by Cold Ion Spectroscopy;The Journal of Physical Chemistry Letters;2023-06-23
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