東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Computational studies of protein sta...

Borreguero, Jose M.

Linked to FindBook

Google Book

Amazon

博客來

Computational studies of protein stability and folding kinetics.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Computational studies of protein stability and folding kinetics./
Author:	Borreguero, Jose M.
Description:	153 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-12, Section: B, page: 6238.
Contained By:	Dissertation Abstracts International65-12B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3157357
ISBN:	9780496901036

Computational studies of protein stability and folding kinetics.
Borreguero, Jose M.

Computational studies of protein stability and folding kinetics. - 153 p.

Source: Dissertation Abstracts International, Volume: 65-12, Section: B, page: 6238.

Thesis (Ph.D.)--Boston University, 2005.

Proteins are some of the most complex systems known, hence to gain a fundamental understanding of their structure and processes will greatly increase our basic knowledge of molecular biology. Computational tools provide a detailed analysis on the atomic scale, though current computers only allow us to study the shortest time-scales. Simplified protein models along with efficient algorithms are currently the best choice for studying protein stability and folding kinetics.

ISBN: 9780496901036Subjects--Topical Terms:

1019105
Biophysics, General.

Computational studies of protein stability and folding kinetics.
LDR:03285nmm 2200313 4500 001 1825130
005 20061206115419.5
008 130610s2005 eng d
020 $a 9780496901036
035 $a (UnM)AAI3157357
035 $a AAI3157357
040 $a UnM $c UnM
100 1 $a Borreguero, Jose M. $3 1914153
245 1 0 $a Computational studies of protein stability and folding kinetics.
300 $a 153 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-12, Section: B, page: 6238.
500 $a Major Professor: H. Eugene Stanley.
502 $a Thesis (Ph.D.)--Boston University, 2005.
520 $a Proteins are some of the most complex systems known, hence to gain a fundamental understanding of their structure and processes will greatly increase our basic knowledge of molecular biology. Computational tools provide a detailed analysis on the atomic scale, though current computers only allow us to study the shortest time-scales. Simplified protein models along with efficient algorithms are currently the best choice for studying protein stability and folding kinetics.
520 $a In our studies of protein stability we employ the multicanonical Monte Carlo algorithm and a coarse-grain protein model to study the protein phase-diagram. We find that the model protein denaturates above the pressure where water freezes to the dense ice phase, in agreement with experiments on bovine pancreatic ribonuclease A. We employ the discrete molecular dynamics algorithm and a series of coarse-grain protein models to study the folding transition at equilibrium conditions. We find that the Src-homology-3 (SH3) proteins resemble a system with only two stable states, mediated by a first-order like transition. In another study, we calculate the stability and structure of the intermediates and the ground state of a designed-peptide by mutating the amino acid sequence. We also study the relevance of electrostatics interactions and the hydrophobic effect in the stability of the decapeptide Abeta(21--30), which has been suggested by recent experiments to be the nucleating site for the formation of the fibrils observed in Alzheimer's disease patients. We find that Abeta(21--30) adopts a loop-like conformation in solution and undergoes partial rearrangement of structure upon aggregation.
520 $a In our studies of folding kinetics we find that the transition state of the SH3 proteins features a set of amino acid contacts that drive the protein to the ground state. Such amino acid contacts are the folding nucleus. We investigate the kinetics of the folding transition of the SH3 proteins over a broad range of temperatures and identify three distinct folding pathways below a specific temperature, the kinetic partition temperature. Our findings suggest the hypothesis that the SH3 proteins, for which only two-state folding kinetics was observed in previous experiments, may exhibit intermediate states under conditions that strongly stabilize the ground state.
590 $a School code: 0017.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Physical. $3 560527
650 4 $a Statistics. $3 517247
690 $a 0786
690 $a 0494
690 $a 0463
710 2 0 $a Boston University. $3 1017454
773 0 $t Dissertation Abstracts International $g 65-12B.
790 1 0 $a Stanley, H. Eugene, $e advisor
790 $a 0017
791 $a Ph.D.
792 $a 2005
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3157357