» Articles » PMID: 22844177

A Peptide's Perspective of Water Dynamics

Overview
Journal Chem Phys
Specialty Chemistry
Date 2012 Jul 31
PMID 22844177
Citations 15
Authors
Affiliations
Soon will be listed here.
Abstract

This Perspective is focused on amide groups of peptides interacting with water. The 2D IR spectroscopy has already enabled structural aspects of the peptide backbone to be determined through its ability to measure the coupling between different amide-I modes. Here we describe why nonlinear IR is emerging as the method of choice to examine the fast components of the water dynamics near peptides and how isotopically edited peptide links can be used to probe the local water at a residue level in proteins. This type of research necessarily involves an intimate mix of theory and experiment. The description of the results is underpinned by relatively well established quantum-statistical theories that describe the important manifestations of peptide vibrational frequency fluctuations.

Citing Articles

A new computational methodology for the characterization of complex molecular environments using IR spectroscopy: bridging the gap between experiments and computations.

Sepulveda-Montano L, Galindo J, Kuroda D Chem Sci. 2024; .

PMID: 39156932 PMC: 11328912. DOI: 10.1039/d4sc03219e.


Probing local changes to α-helical structures with 2D IR spectroscopy and isotope labeling.

Webb K, Hess K, Shmidt A, Segner K, Buchanan L Biophys J. 2023; 122(8):1491-1502.

PMID: 36906800 PMC: 10147839. DOI: 10.1016/j.bpj.2023.03.014.


Bottom-Up Approach to Assess the Molecular Structure of Aqueous Poly(-Isopropylacrylamide) at Room Temperature via Infrared Spectroscopy.

Gobeze H, Ma J, Leonik F, Kuroda D J Phys Chem B. 2020; 124(51):11699-11710.

PMID: 33306373 PMC: 7872429. DOI: 10.1021/acs.jpcb.0c08424.


The Amide I Spectrum of Proteins-Optimization of Transition Dipole Coupling Parameters Using Density Functional Theory Calculations.

Baronio C, Barth A J Phys Chem B. 2020; 124(9):1703-1714.

PMID: 32040320 PMC: 7307917. DOI: 10.1021/acs.jpcb.9b11793.


Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules.

Tan J, Zhang J, Li C, Luo Y, Ye S Nat Commun. 2019; 10(1):1010.

PMID: 30824834 PMC: 6397197. DOI: 10.1038/s41467-019-08899-3.


References
1.
Fecko C, Loparo J, Roberts S, Tokmakoff A . Local hydrogen bonding dynamics and collective reorganization in water: ultrafast infrared spectroscopy of HOD/D(2)O. J Chem Phys. 2005; 122(5):54506. DOI: 10.1063/1.1839179. View

2.
Laage D, Hynes J . Echoes of a salty exchange. Proc Natl Acad Sci U S A. 2009; 106(4):967-8. PMC: 2633541. DOI: 10.1073/pnas.0812306106. View

3.
Renthal R . Buried water molecules in helical transmembrane proteins. Protein Sci. 2007; 17(2):293-8. PMC: 2222723. DOI: 10.1110/ps.073237508. View

4.
Ghosh A, Qiu J, DeGrado W, Hochstrasser R . Tidal surge in the M2 proton channel, sensed by 2D IR spectroscopy. Proc Natl Acad Sci U S A. 2011; 108(15):6115-20. PMC: 3076828. DOI: 10.1073/pnas.1103027108. View

5.
Garrett-Roe S, Hamm P . What can we learn from three-dimensional infrared spectroscopy?. Acc Chem Res. 2009; 42(9):1412-22. DOI: 10.1021/ar900028k. View