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LEADER 03184cam a2200493Ii 4500

001 on1097606096;

003 OCoLC;

005 20190508040801.0;

006 m o d ;

007 cr unu||||||||;

008 190418s2018 ncua obm 000 0 eng d;

035 a| (Sirsi) o1097606096;

035 a| (OCoLC)1097606096;

049 a| EREE;

090 a| TA1522;

100 1 a| Kuyateh, Abu-Bakarr,e| author.?| UNAUTHORIZED;

245 14 a| The development of beta-actin mutants with altered binding affinites for ATP and ADP /c| by Abu-Bakarr Kuyateh.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2018.;

300 a| 65 pages :b| illustrations (chiefly color);

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 3.113 MB2| rda;

538 a| System requirements: Adobe Reader.;

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

502 b| M.S.c| East Carolina Universityd| 2018.;

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

500 a| Advisor: Robert Hughes;

500 a| Title from PDF t.p. (viewed April 26, 2019).;

520 3 a| A number of neurodegenerative diseases are accompanied by the formation of cofilin-actin rods in neural cells. These rods can cause synaptic dysfunction and block transport within neurites. The overall goal of this project is to create an optogenetic switch that incorporates both cofilin (an actin-binding protein) and actin for the study of cofilin-actin rod formation in neural cells undergoing oxidative stress. During the course of the work, a protocol has been created to express the protein [beta]-actin. Protein overexpression and purification, circular dichroism, mass spectrometry, and electrophoresis have been utilized to isolate and characterize [beta]-actin. Site-directed mutagenesis has been conducted to create a series of mutants to explore which residues are key for nucleotide binding. A number of challenges related to protein expression and stability of this protein precluded completion of these studies. As a result, we turned to mutants of optogenetic actin to study nucleotide binding in cells. The results from these studies indicate that point mutants in our actin construct, in conjunction with an optogenetic cofilin, can provide insight into the nucleotide binding state of actin under different oxidant concentrations.;

504 a| Includes bibliographical references.;

650 0 a| Optogenetics.=| ^A1380192;

650 0 a| Mutagenesis.=| ^A85718;

650 0 a| Microfilament proteins.=| ^A249566;

700 1 a| Hughes, Robert,e| degree supervisor.=| ^A61249;

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

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/7027;

949 o| wjh;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 5091104;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5091104-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 4/18/2019x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5091104-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 4/18/2019x| ETDz| HERESOURCE;

The development of beta-actin mutants with altered binding affinites for ATP and ADP / by Abu-Bakarr Kuyateh.

Author/creator	Kuyateh, Abu-Bakarr author.
Other author	Hughes, Robert, degree supervisor.
Other author	East Carolina University. Department of Chemistry.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2018.
Description	65 pages : illustrations (chiefly color)
Supplemental Content	Access via ScholarShip
Subjects	Optogenetics. Mutagenesis. Microfilament proteins.

Summary	A number of neurodegenerative diseases are accompanied by the formation of cofilin-actin rods in neural cells. These rods can cause synaptic dysfunction and block transport within neurites. The overall goal of this project is to create an optogenetic switch that incorporates both cofilin (an actin-binding protein) and actin for the study of cofilin-actin rod formation in neural cells undergoing oxidative stress. During the course of the work, a protocol has been created to express the protein [beta]-actin. Protein overexpression and purification, circular dichroism, mass spectrometry, and electrophoresis have been utilized to isolate and characterize [beta]-actin. Site-directed mutagenesis has been conducted to create a series of mutants to explore which residues are key for nucleotide binding. A number of challenges related to protein expression and stability of this protein precluded completion of these studies. As a result, we turned to mutants of optogenetic actin to study nucleotide binding in cells. The results from these studies indicate that point mutants in our actin construct, in conjunction with an optogenetic cofilin, can provide insight into the nucleotide binding state of actin under different oxidant concentrations.
General note	Presented to the faculty of the Department of Chemistry
General note	Advisor: Robert Hughes
General note	Title from PDF t.p. (viewed April 26, 2019).
Dissertation note	M.S. East Carolina University 2018.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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The development of beta-actin mutants with altered binding affinites for ATP and ADP / by Abu-Bakarr Kuyateh.

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