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Title:Structural Characterization of the Amino- and Carboxy -Terminal Domains of Troponin C by High Pressure Nuclear Magnetic Resonance
Author(s):Yu, Aimee Cu
Doctoral Committee Chair(s):Jonas, Ana; Jonas, Jiri
Department / Program:Biochemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Subject(s):Chemistry, Biochemistry
Abstract:Our main research objective is to investigate the effects of high pressure on the structure, stability, and dynamics of proteins. The application of pressure provides a unique method to reversibly unfold proteins. Pressure is a gentler method of denaturation than other more traditional methods and also has the added benefit of generating a more concise thermodynamic description of the system. In our lab, one- and two-dimensional proton nuclear magnetic resonance is utilized to observe pressure-induced conformational changes and to isolate possible folding intermediates in proteins. Other techniques, such as computer simulations, circular dichroism, and fluorescence, are also utilized to obtain additional information. Through the use of a variety of spectroscopic techniques, the stability and folding pathways of proteins can be characterized.
Issue Date:2000
Description:211 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000.
Other Identifier(s):(MiAaPQ)AAI9990200
Date Available in IDEALS:2015-09-25
Date Deposited:2000

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