Tools

LEADER 03329cam 2200613Ii 4500

001 ocn919448354;

003 OCoLC;

005 20160202100010.0;

006 m o d ;

007 cr bn|||||||||;

008 150831s2015 ncua ob 000 0 eng d;

035 a| (Sirsi) o919448354;

035 a| (OCoLC)919448354;

049 a| EREE;

090 a| QD181.C3;

100 1 a| Fulcher, Lindsay Michelle,e| author.?| UNAUTHORIZED;

245 10 a| Thermodynamic and spectroscopic studies of Cd²⁺ binding to the regulatory domain and full length human cardiac troponin C (HcTnC) :b| elucidating plausible Cd²⁺ binding sites /c| by Lindsay Michelle Fulcher.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2015.;

300 a| 119 pages :b| color illustrations;

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 1.84Mb2| rda;

538 a| System requirements: Adobe Reader.;

538 a| Mode of access: World Wide Web.;

502 b| M.S.c| East Carolina Universityd| 2015.;

500 a| Presented to the faculty of the Department of Chemistry.;

500 a| Advisor: Anne M. Spuches.;

500 a| Title from PDF t.p. (viewed September 21, 2015).;

520 3 a| Toxic metals such as cadmium (Cd²⁺) have been shown to bind to and interfere with various calcium (Ca²⁺) binding proteins including the regulatory protein cardiac troponin C (cTnC). Recent structural data has shown that Cd²⁺ binds to both EF hand Ca²⁺ binding loops in the regulatory N-domain of human cTnC including EF hand loop I, which normally does not bind metal. Although the data reveal two Cd²⁺ ions bound to the protein, the binding constants and other thermodynamic parameters are not known. Therefore, the goal of this research project is to use Isothermal Titration Calorimetry (ITC) to obtain thermodynamic parameters such as K, [delta]H, [delta]G and [delta]S of Cd²⁺ binding to both the full length and N-domain (amino acid residues 1-89) of HcTnC and compare the parameters to our previous data with Ca²⁺. Through our results we hope to shed light on potential mechanisms of cadmium toxicity.;

504 a| Includes bibliographical references.;

650 0 a| Cadmiumx| Isotopes.=| ^A1279645;

650 0 a| Calciumx| Isotopes.=| ^A1279646;

650 0 a| Heavy metals.=| ^A51950;

650 0 a| Calcium-binding proteins.=| ^A11644;

650 0 a| Calorimetry.=| ^A17772;

653 a| Biochemistry;

653 a| Inorganic chemistry;

653 a| Bioinorganic chemistry;

653 a| Circular dichroism;

653 a| EF hands;

653 a| HcTnC;

653 a| Isothermal titration calorimetry;

653 a| Toxic metals;

700 1 a| Spuches, Anne M.,e| degree supervisor.?| UNAUTHORIZED;

710 2 a| East Carolina University.b| Department of Chemistry.?| UNAUTHORIZED;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/5009;

949 o| jgml;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 3808151;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 3808151-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 8/31/2015x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 3808151-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 8/31/2015x| ETDz| HERESOURCE;

Thermodynamic and spectroscopic studies of Cd²⁺ binding to the regulatory domain and full length human cardiac troponin C (HcTnC) : elucidating plausible Cd²⁺ binding sites / by Lindsay Michelle Fulcher.

Author/creator	Fulcher, Lindsay Michelle author.
Other author	Spuches, Anne M., degree supervisor.
Other author	East Carolina University. Department of Chemistry.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2015.
Description	119 pages : color illustrations
Supplemental Content	Access via ScholarShip
Subjects	Cadmium--Isotopes. Calcium--Isotopes. Heavy metals. Calcium-binding proteins. Calorimetry.

Summary	Toxic metals such as cadmium (Cd²⁺) have been shown to bind to and interfere with various calcium (Ca²⁺) binding proteins including the regulatory protein cardiac troponin C (cTnC). Recent structural data has shown that Cd²⁺ binds to both EF hand Ca²⁺ binding loops in the regulatory N-domain of human cTnC including EF hand loop I, which normally does not bind metal. Although the data reveal two Cd²⁺ ions bound to the protein, the binding constants and other thermodynamic parameters are not known. Therefore, the goal of this research project is to use Isothermal Titration Calorimetry (ITC) to obtain thermodynamic parameters such as K, [delta]H, [delta]G and [delta]S of Cd²⁺ binding to both the full length and N-domain (amino acid residues 1-89) of HcTnC and compare the parameters to our previous data with Ca²⁺. Through our results we hope to shed light on potential mechanisms of cadmium toxicity.
General note	Presented to the faculty of the Department of Chemistry.
General note	Advisor: Anne M. Spuches.
General note	Title from PDF t.p. (viewed September 21, 2015).
Dissertation note	M.S. East Carolina University 2015.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

Thermodynamic and spectroscopic studies of Cd²⁺ binding to the regulatory domain and full length human cardiac troponin C (HcTnC) : elucidating plausible Cd²⁺ binding sites / by Lindsay Michelle Fulcher.

Click here for more information about this title