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

Molecular dynamics study of alpha-he...

Rosencrance, Susan M.

Linked to FindBook

Google Book

Amazon

博客來

Molecular dynamics study of alpha-helical coiled-coils: Hydrophobic interactions and their impact on helix orientation and coiled-coil stability.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Molecular dynamics study of alpha-helical coiled-coils: Hydrophobic interactions and their impact on helix orientation and coiled-coil stability./
Author:	Rosencrance, Susan M.
Description:	112 p.
Notes:	Chair: Frederick W. Carson.
Contained By:	Dissertation Abstracts International63-03B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048286
ISBN:	0493624007

Molecular dynamics study of alpha-helical coiled-coils: Hydrophobic interactions and their impact on helix orientation and coiled-coil stability.
Rosencrance, Susan M.

Molecular dynamics study of alpha-helical coiled-coils: Hydrophobic interactions and their impact on helix orientation and coiled-coil stability. - 112 p.

Chair: Frederick W. Carson.

Thesis (Ph.D.)--The American University, 2002.

The two-stranded α-helical coiled-coil found in the enzyme seryl t-RNA synthetase (STS) folds as an antiparallel coiled-coil, the typical orientation for coiled-coils in globular proteins. On the other hand coiled-coils found in DNA-binding proteins like GCN4 typically maintain a parallel orientation. This study addresses the following questions: what role do hydrophobic interactions play in influencing the orientation of helices in a coiled-coil and what impact do they have on coiled-coil stability?

ISBN: 0493624007Subjects--Topical Terms:

1019105
Biophysics, General.

Molecular dynamics study of alpha-helical coiled-coils: Hydrophobic interactions and their impact on helix orientation and coiled-coil stability.
LDR:02860nam 2200301 a 45 001 935361
005 20110509
008 110509s2002 eng d
020 $a 0493624007
035 $a (UnM)AAI3048286
035 $a AAI3048286
040 $a UnM $c UnM
100 1 $a Rosencrance, Susan M. $3 1259050
245 1 0 $a Molecular dynamics study of alpha-helical coiled-coils: Hydrophobic interactions and their impact on helix orientation and coiled-coil stability.
300 $a 112 p.
500 $a Chair: Frederick W. Carson.
500 $a Source: Dissertation Abstracts International, Volume: 63-03, Section: B, page: 1350.
502 $a Thesis (Ph.D.)--The American University, 2002.
520 $a The two-stranded α-helical coiled-coil found in the enzyme seryl t-RNA synthetase (STS) folds as an antiparallel coiled-coil, the typical orientation for coiled-coils in globular proteins. On the other hand coiled-coils found in DNA-binding proteins like GCN4 typically maintain a parallel orientation. This study addresses the following questions: what role do hydrophobic interactions play in influencing the orientation of helices in a coiled-coil and what impact do they have on coiled-coil stability?
520 $a The molecular dynamics program CHARMm was used to build parallel and antiparallel models of the STS and GCN4 coiled-coils <italic>in vacuo</italic> and to evaluate the influence of hydrophobic interactions. Native models of the STS antiparallel coiled-coil and the GCN4 parallel coiled-coil, based on the x-ray crystallographic structures, were compared to designed models of a STS parallel and a GCN4 antiparallel coiled-coil. Differences in hydrophobic packing and residue accessibility in each orientation were evaluated using the Lee and Richards method. Also, solvation free energies calculated using the Eisenberg and McLachlan method were used to predict the relative stability of each orientation in terms of hydrophobic interactions.
520 $a The results showed the antiparallel orientation was the preferred orientation for a two-stranded α-helical coiled-coil in terms of hydrophobic packing and residue accessibility. Furthermore solvation free energy calculations showed the antiparallel orientation was more stable in terms of hydrophobic interactions than its parallel counterpart. Thus, these results suggest that while hydrophobic interactions in isolation dictate an antiparallel orientation, there are other overriding factors such as electrostatics that ultimately determine the parallel orientation of coiled-coils found in DNA-binding proteins.
590 $a School code: 0008.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0487
690 $a 0786
710 2 0 $a The American University. $3 1017567
773 0 $t Dissertation Abstracts International $g 63-03B.
790 $a 0008
790 1 0 $a Carson, Frederick W., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048286