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Theoretical studies in protein foldi...

Karanicolas, John.

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Theoretical studies in protein folding: WW domains.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Theoretical studies in protein folding: WW domains./
作者:	Karanicolas, John.
面頁冊數:	190 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3103.
Contained By:	Dissertation Abstracts International64-07B.
標題:	Biology, Molecular. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3097077

Theoretical studies in protein folding: WW domains.
Karanicolas, John.

Theoretical studies in protein folding: WW domains. - 190 p.

Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3103.

Thesis (Ph.D.)--The Scripps Research Institute, 2003.

Many proteins must adopt a single stable conformation from a vast number of possibilities in order to perform their function. Progress in the last thirty years of studying the process of folding has resulted in useful insights in understanding diseases related to protein misfolding, in protein design, and in the prediction of protein structure from sequence. Theoretical studies of protein folding have typically focused on elucidating general features of folding, rather than understanding phenomena relating to specific proteins. Now that many of these general features are understood, specific proteins which display unusual behavior may be identified and examined in detail. Because it is function which drives the evolution of proteins, it should be possible to rationalize observed folding behavior on the basis of function. This in turn may provide insight into the rationale behind this product of evolution, which may ultimately be used in the design of functional proteins.Subjects--Topical Terms:

1017719
Biology, Molecular.

Theoretical studies in protein folding: WW domains.
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245 1 0 $a Theoretical studies in protein folding: WW domains.
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500 $a Source: Dissertation Abstracts International, Volume: 64-07, Section: B, page: 3103.
500 $a Adviser: Charles L. Brooks, III.
502 $a Thesis (Ph.D.)--The Scripps Research Institute, 2003.
520 $a Many proteins must adopt a single stable conformation from a vast number of possibilities in order to perform their function. Progress in the last thirty years of studying the process of folding has resulted in useful insights in understanding diseases related to protein misfolding, in protein design, and in the prediction of protein structure from sequence. Theoretical studies of protein folding have typically focused on elucidating general features of folding, rather than understanding phenomena relating to specific proteins. Now that many of these general features are understood, specific proteins which display unusual behavior may be identified and examined in detail. Because it is function which drives the evolution of proteins, it should be possible to rationalize observed folding behavior on the basis of function. This in turn may provide insight into the rationale behind this product of evolution, which may ultimately be used in the design of functional proteins.
520 $a Topology, or structure, has been shown to be a determinant of many protein folding properties. In order to better understand the effect of protein sequence beyond its role in facilitating topology, my studies began with the development of a procedure to build simple protein models which capture more than merely topology. These models are then used to examine differences between specific proteins of shared topology.
520 $a The work presented in this thesis culminates with an examination of WW domains, a series of structurally related protein modules involved in signaling. Experimentally described differences in the folding of specific WW domains are rationalized: first at the amino-acid level via the simple model developed to explore the effect of sequence differences in topologically analogous proteins, and subsequently at atomic level resolution using a more detailed model. The features which lead to unusual folding properties in one of the WW domains are explained as a direct product of the functional requirements upon this protein module.
590 $a School code: 1179.
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650 4 $a Biophysics, General. $3 1019105
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791 $a Ph.D.
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