Document Type

Thesis

Degree

Master of Science (MS)

Department

Chemistry

First Advisor's Name

Jaroslava Miksovska

First Advisor's Committee Title

Committee Chair

Second Advisor's Name

David C. Chatfield

Third Advisor's Name

Xiaotang Wang

Date of Defense

7-8-2010

Abstract

The Ca2+ association to calcium binding proteins (CaBPs) represents an essential step in Ca2+ signal transduction. This study presents a characterization of Ca interactions with two CaBPs, calmodulin and DREAM, using time-resolved photothermal and fluorescence techniques. Calcium binding to the calmodulin C-terminal domain is associated with a volume change of 40 mL mol-1and an enthalpy change of 35 ± 16 kcal mol-1. These parameters are consistent with the Ca2+ triggered exposure of hydrophobic patches on the calmodulin surface. Also, the rate limiting step for Ca2+ binding to calmodulin is the closed-to-open transition of the C-terminal domain that occurs with a lifetime of 400 μs. Unlike calmodulin, DREAM exists in a dynamic equilibrium of two conformations and Ca2+ binding shifts the equilibrium towards a more compact conformation. These data clearly demonstrate that conformational dynamics play a crucial role in the transmission of Ca2+ signals.

Identifier

FI14062264

Comments

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Included in

Chemistry Commons

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