Tools

LEADER 03203cam 2200517Ii 4500

001 on1231501233;

003 OCoLC;

005 20210629035347.0;

006 m o d ;

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

008 210114s2020 ncua obm 000 0 eng d;

035 a| (Sirsi) o1231501233;

035 a| (OCoLC)1231501233;

049 a| EREE;

090 a| QP552.C6;

100 1 a| Banzon, Patrick Daniel,e| author.?| UNAUTHORIZED;

245 10 a| How charged residues influence the thermal stability of collagen :b| a study with natural and non-natural amino acids /c| by Patrick Daniel Banzon.;

264 1 a| [Greenville, N.C.] :b| [East Carolina University],c| 2020.;

300 a| 103 pages :b| illustrations (some color);

336 a| textb| txt2| rdacontent;

337 a| computerb| c2| rdamedia;

338 a| online resourceb| cr2| rdacarrier;

347 a| text fileb| PDFc| 12.63 MB2| rda;

538 a| System requirements: Adobe Reader.;

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

502 b| M.S.c| East Carolina Universityd| 2020.;

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

500 a| Advisor: William E. Allen;

500 a| Title from PDF t.p. (June 16, 2021).;

520 3 a| Triple-helical collagens are key structural proteins in mammals. Their ubiquity and diverse functions drive our interest into understanding their behavior at a fundamental level. This thesis describes a reductionist approach using novel collagen-related peptides (CRPs), into which one or more electrical charges have been imparted at known positions. One series of CRPs includes fluorescent pyrene tags at their N-termini, directly adjacent to the charged residues lysine (Lys, K) and glutamic acid (Glu, E). When in close contact, the fluorophores form excimers that emit low-energy light. Monitoring of the excimer intensity shows that nucleation of collagen peptides is critically dependent on the charge location. Another series of CRPs features pH-independent (permanent) positive charge close to the peptide backbone, via a synthetic proline derivative called "Map." When in close contact, repulsion between Map residues overwhelms the natural tendencies of the peptides to fold. CD and fluorescence investigations into the thermodynamic and kinetic behaviors of these CRPs have been supplemented with computational analyses, to shed light on the deleterious role of charge in trimer formation.;

504 a| Includes bibliographical references.;

650 0 a| Collagen.=| ^A4169;

650 0 a| Peptides.=| ^A3253;

650 0 a| Amino acids.=| ^A6734;

653 a| Thermal Stability;

653 a| Charge;

700 1 a| Allen, William E.,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/10342/8821;

949 o| wjh;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 5547845;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5547845-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 1/14/2021x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 5547845-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 1/14/2021x| ETDz| HERESOURCE;

How charged residues influence the thermal stability of collagen : a study with natural and non-natural amino acids / by Patrick Daniel Banzon.

Author/creator	Banzon, Patrick Daniel author.
Other author	Allen, William E., degree supervisor.
Other author	East Carolina University. Department of Chemistry.
Format	Theses and dissertations
Publication	[Greenville, N.C.] : [East Carolina University], 2020.
Description	103 pages : illustrations (some color)
Supplemental Content	Access via ScholarShip
Subjects	Collagen. Peptides. Amino acids.

Summary	Triple-helical collagens are key structural proteins in mammals. Their ubiquity and diverse functions drive our interest into understanding their behavior at a fundamental level. This thesis describes a reductionist approach using novel collagen-related peptides (CRPs), into which one or more electrical charges have been imparted at known positions. One series of CRPs includes fluorescent pyrene tags at their N-termini, directly adjacent to the charged residues lysine (Lys, K) and glutamic acid (Glu, E). When in close contact, the fluorophores form excimers that emit low-energy light. Monitoring of the excimer intensity shows that nucleation of collagen peptides is critically dependent on the charge location. Another series of CRPs features pH-independent (permanent) positive charge close to the peptide backbone, via a synthetic proline derivative called "Map." When in close contact, repulsion between Map residues overwhelms the natural tendencies of the peptides to fold. CD and fluorescence investigations into the thermodynamic and kinetic behaviors of these CRPs have been supplemented with computational analyses, to shed light on the deleterious role of charge in trimer formation.
General note	Presented to the Faculty of the Department of Chemistry
General note	Advisor: William E. Allen
General note	Title from PDF t.p. (June 16, 2021).
Dissertation note	M.S. East Carolina University 2020.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

Availability

Library	Location	Call Number	Status	Item Actions
	Electronic Resources	Access Content Online	✔ Available

How charged residues influence the thermal stability of collagen : a study with natural and non-natural amino acids / by Patrick Daniel Banzon.

Click here for more information about this title

Availability