Ultrafast Solvation Dynamics of Human Serum Albumin: Correlations with Conformational Transitions and Site-Selected Recognition-Reference-Cited by-同舟云学术

Ultrafast Solvation Dynamics of Human Serum Albumin: Correlations with Conformational Transitions and Site-Selected Recognition

Published:2006-04-08 Issue:21 Volume:110 Page:10540-10549
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Qiu Weihong¹,Zhang Luyuan¹,Okobiah Oghaghare¹,Yang Yi¹,Wang Lijuan¹,Zhong Dongping¹,Zewail Ahmed H.²

Affiliation:

1. Departments of Physics, Chemistry, and Biochemistry, Programs of Biophysics, Chemical Physics, and Biochemistry, 191 West Woodruff Avenue, The Ohio State University, Columbus, Ohio 43210

2. Laboratory for Molecular Sciences, Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena, California 91125

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/jp055989w

Reference48 articles.

1. Dynamics of Water in Biological Recognition

2. Protein–water interactions in a dynamic world

3. Slaving: Solvent fluctuations dominate protein dynamics and functions

4. Femtosecond dynamics of rubredoxin: Tryptophan solvation and resonance energy transfer in the protein

5. Biological water at the protein surface: Dynamical solvation probed directly with femtosecond resolution

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