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Time-resolved infrared and fluoresce...

Serrano, Arnaldo L.

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Time-resolved infrared and fluorescence spectroscopic studies of protein dynamics and structure.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Time-resolved infrared and fluorescence spectroscopic studies of protein dynamics and structure./
Author:	Serrano, Arnaldo L.
Description:	199 p.
Notes:	Source: Dissertation Abstracts International, Volume: 74-10(E), Section: B.
Contained By:	Dissertation Abstracts International74-10B(E).
Subject:	Physical chemistry. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3565227
ISBN:	9781303147722

Time-resolved infrared and fluorescence spectroscopic studies of protein dynamics and structure.
Serrano, Arnaldo L.

Time-resolved infrared and fluorescence spectroscopic studies of protein dynamics and structure. - 199 p.

Source: Dissertation Abstracts International, Volume: 74-10(E), Section: B.

Thesis (Ph.D.)--University of Pennsylvania, 2013.

While the structure of a particular folded protein is a direct outcome of the underlying thermodynamics, arriving at a quantitative and predictive understanding of how this folded structure is reached nevertheless poses huge challenges. Among those challenges is the need for probes of protein folding that possess both high temporal and structural resolution. To this end, this Thesis reports studies performed on a number of model peptide and protein systems aimed at applying novel spectroscopic techniques and molecular probes to the task of acquiring highly detailed information about either the mechanism of folding or the nature of the native protein structure.

ISBN: 9781303147722Subjects--Topical Terms:

1981412
Physical chemistry.

Time-resolved infrared and fluorescence spectroscopic studies of protein dynamics and structure.
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100 1 $a Serrano, Arnaldo L. $3 3191504
245 1 0 $a Time-resolved infrared and fluorescence spectroscopic studies of protein dynamics and structure.
300 $a 199 p.
500 $a Source: Dissertation Abstracts International, Volume: 74-10(E), Section: B.
500 $a Adviser: Feng Gai.
502 $a Thesis (Ph.D.)--University of Pennsylvania, 2013.
520 $a While the structure of a particular folded protein is a direct outcome of the underlying thermodynamics, arriving at a quantitative and predictive understanding of how this folded structure is reached nevertheless poses huge challenges. Among those challenges is the need for probes of protein folding that possess both high temporal and structural resolution. To this end, this Thesis reports studies performed on a number of model peptide and protein systems aimed at applying novel spectroscopic techniques and molecular probes to the task of acquiring highly detailed information about either the mechanism of folding or the nature of the native protein structure.
520 $a The earlier chapters of this Thesis present studies on the utility of the artificial amino-acid p-cyanophenylalanine as a time-resolved fluorescence and energy-transfer probe of local protein structure. Application of this probe to the villin headpiece subdomain revealed new details about the native state ensemble of this mini-protein.
520 $a The later chapters report the findings of a number of time-resolved laser temperature-jump experiments on model helical peptides as well as on the mini-protein Trp-Cage. These experiments provide benchmarks for some of the elementary kinetic events of helix formation for the former and detailed insight into the folding mechanism of one of the fastest folding proteins known to date for the latter.
590 $a School code: 0175.
650 4 $a Physical chemistry. $3 1981412
650 4 $a Biophysics. $3 518360
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710 2 $a University of Pennsylvania. $b Chemistry. $3 2096482
773 0 $t Dissertation Abstracts International $g 74-10B(E).
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791 $a Ph.D.
792 $a 2013
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3565227