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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.

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Experimental study of single protein mechanics and protein rates of unfolding./
作者:	Hermans, Rodolfo I.
面頁冊數:	276 p.
附註:	Source: Dissertation Abstracts International, Volume: 71-03, Section: B, page: 1760.
Contained By:	Dissertation Abstracts International71-03B.
標題:	Physics, Condensed Matter. -
電子資源:	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.
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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.
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