Fast dynamics of aqueous biological molecules investigated with 2D IR spectroscopy

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Abstract/Contents

Abstract
Proteins are dynamic structures that are in constant fluctuations, and their ability to undergo structural changes is critical to their function. However, their fastest dynamics in thermal equilibrium have remained largely unexplored. In this work, studies that examine the dynamics of aqueous proteins using two-dimensional infrared echo spectroscopy (2D IR) are presented. In particular, investigations of fast fluctuations in proteins and peptides within the context of structural changes upon denaturation are discussed. 2D IR is a nonlinear optical spectroscopic technique that can measure ultrafast dynamics of complex molecules in the picoseconds regime, timescales ~6-10 orders of magnitude faster than nuclear magnetic resonance. In addition, the relatively low energy mid-IR laser pulses used in this study probe the relevant nuclear degrees of freedom without significantly perturbing the protein structure or dynamics. Brief descriptions of the experimental setup and methods, as well as analysis and interpretation, are given.

Description

Type of resource text
Form electronic; electronic resource; remote
Extent 1 online resource.
Publication date 2012
Issuance monographic
Language English

Creators/Contributors

Associated with Chung, Jean K
Associated with Stanford University, Department of Chemistry
Primary advisor Fayer, Michael D
Thesis advisor Fayer, Michael D
Thesis advisor Andersen, Hans, 1941-
Thesis advisor Dai, Hongjie, 1966-
Advisor Andersen, Hans, 1941-
Advisor Dai, Hongjie, 1966-

Subjects

Genre Theses

Bibliographic information

Statement of responsibility Jean K. Chung.
Note Submitted to the Department of Chemistry.
Thesis Thesis (Ph.D.)--Stanford University, 2012.
Location electronic resource

Access conditions

Copyright
© 2012 by Jean K Chung
License
This work is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported license (CC BY-NC).

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