University of Illinois Urbana-Champaign

Structural Characterization of the Amino- and Carboxy -Terminal Domains of Troponin C by High Pressure Nuclear Magnetic Resonance

Yu, Aimee Cu

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Description

Title
Structural Characterization of the Amino- and Carboxy -Terminal Domains of Troponin C by High Pressure Nuclear Magnetic Resonance
Author(s)
Yu, Aimee Cu
Issue Date
2000
Doctoral Committee Chair(s)
  • Jonas, Ana
  • Jonas, Jiri
Department of Study
Biochemistry
Discipline
Biochemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
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.
Graduation Semester
2000
Type of Resource
text
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http://hdl.handle.net/2142/84921

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