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Experimental study of single protein...

Hermans, Rodolfo I.

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Experimental study of single protein mechanics and protein rates of unfolding.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Experimental study of single protein mechanics and protein rates of unfolding./
Author:	Hermans, Rodolfo I.
Description:	276 p.
Notes:	Source: Dissertation Abstracts International, Volume: 71-03, Section: B, page: 1760.
Contained By:	Dissertation Abstracts International71-03B.
Subject:	Physics, Condensed Matter. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3400547
ISBN:	9781109673784

Experimental study of single protein mechanics and protein rates of unfolding.
Hermans, Rodolfo I.

Experimental study of single protein mechanics and protein rates of unfolding. - 276 p.

Source: Dissertation Abstracts International, Volume: 71-03, Section: B, page: 1760.

Thesis (Ph.D.)--Columbia University, 2010.

This dissertation is a multidisciplinary approach to the understanding of the mechanical properties of proteins and their kinetics of unfolding, through the use of an atomic force microscope in force-clamp mode to perform single-molecule force spectroscopy. It begins with the development of a new experimental framework, which includes the design and construction of a new faster atomic force microscopy instrumentation, the definition of new bias-free experimental protocols, and the application of modern statistical tools for data analysis, all of these optimized for the use in force spectroscopy at the single molecule level. Through this new framework new insight was gained on the laws governing the mechanics of a protein in solution. The kinetics of unfolding of the protein ubiquitin were experimentally observed to feature a broad power-law distribution of unfolding rates, quality characteristic of glassy kinetics, which challenges the commonly accepted simplest single rate two-state model models for protein unfolding. Also, the transition between two highly stretched structural configurations of a protein was directly observed to be rate-limited, revealing the magnitude of the intrinsic friction limiting the speed of the first stage of protein folding. This document is presented with detailed technical and mathematical considerations with the intention to serve as handbook for the experimentalist interested in the study of polymers using force-clamp single molecule force spectroscopy.

ISBN: 9781109673784Subjects--Topical Terms:

1018743
Physics, Condensed Matter.

Experimental study of single protein mechanics and protein rates of unfolding.
LDR:02403nam 2200277 4500 001 1392546
005 20110218114608.5
008 130515s2010 ||||||||||||||||| ||eng d
020 $a 9781109673784
035 $a (UMI)AAI3400547
035 $a AAI3400547
040 $a UMI $c UMI
100 1 $a Hermans, Rodolfo I. $3 1671004
245 1 0 $a Experimental study of single protein mechanics and protein rates of unfolding.
300 $a 276 p.
500 $a Source: Dissertation Abstracts International, Volume: 71-03, Section: B, page: 1760.
500 $a Adviser: Julio M. Fernandez.
502 $a Thesis (Ph.D.)--Columbia University, 2010.
520 $a This dissertation is a multidisciplinary approach to the understanding of the mechanical properties of proteins and their kinetics of unfolding, through the use of an atomic force microscope in force-clamp mode to perform single-molecule force spectroscopy. It begins with the development of a new experimental framework, which includes the design and construction of a new faster atomic force microscopy instrumentation, the definition of new bias-free experimental protocols, and the application of modern statistical tools for data analysis, all of these optimized for the use in force spectroscopy at the single molecule level. Through this new framework new insight was gained on the laws governing the mechanics of a protein in solution. The kinetics of unfolding of the protein ubiquitin were experimentally observed to feature a broad power-law distribution of unfolding rates, quality characteristic of glassy kinetics, which challenges the commonly accepted simplest single rate two-state model models for protein unfolding. Also, the transition between two highly stretched structural configurations of a protein was directly observed to be rate-limited, revealing the magnitude of the intrinsic friction limiting the speed of the first stage of protein folding. This document is presented with detailed technical and mathematical considerations with the intention to serve as handbook for the experimentalist interested in the study of polymers using force-clamp single molecule force spectroscopy.
590 $a School code: 0054.
650 4 $a Physics, Condensed Matter. $3 1018743
650 4 $a Biophysics, General. $3 1019105
690 $a 0611
690 $a 0786
710 2 $a Columbia University. $3 571054
773 0 $t Dissertation Abstracts International $g 71-03B.
790 1 0 $a Fernandez, Julio M., $e advisor
790 $a 0054
791 $a Ph.D.
792 $a 2010
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3400547