Thermal unfolding dynamics of proteins probed by nonlinear infrared spectroscopy

This thesis presents spectroscopic approaches to study the thermal unfolding dynamics of proteins. The spectroscopic tool is nonlinear infrared (IR) spectroscopy of the protein amide I band. Among various nonlinear IR techniques, two-dimensional infrared (2D IR) spectroscopy, which is an IR analogue of 2D NMR, is the most informative. A 2D IR spectrum is obtained from a double Fourier transform of the heterodyned third-order nonlinear signal, which is generated by three consecutive interactions between femtosecond IR pulses and the vibrations of the system. This technique is sensitive to the presence of P-sheet structure in proteins through the formation of cross peaks between the two characteristic vibrational modes of 0-sheets. In this work, 2D IR spectroscopy is used to measure equilibrium thermal unfolding of ribonuclease A and ubiquitin. For transient unfolding studies, the temperature of the solution is rapidly raised by a nanosecond temperature jump (T-jump) laser, which is followed by probing structural changes of proteins with dispersed vibrational echo (DVE) spectroscopy or 2D IR spectroscopy.

Department dc:contributor.department

Massachusetts Institute of Technology. Dept. of Chemistry.

Grantor dc:publisher

Massachusetts Institute of Technology

Year dc:date.issued

2007

Author dc:creator

• Chung, Hoi Sung

Advisor dc:contributor.advisor

• Andrei Tokmakoff.

• Chemistry.

Statement dc:rights

• M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.

Licence dc:rights.uri

• http://dspace.mit.edu/handle/1721.1/7582

Language dc:language.iso

eng

Handle dc:identifier.uri

http://hdl.handle.net/1721.1/38617

OAI identifier oai:identifier

oai:dspace.mit.edu:1721.1/38617