東華大學圖書館 |

Language: English

Back

Switch To: Labeled | MARC Mode | ISBD

Characterization of the long-range s...

Ackerman, Michael Scott, Jr.

Amazon

博客來

Characterization of the long-range structure of the denatured state of staphylococcal nuclease through the analysis of residual dipolar couplings.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Characterization of the long-range structure of the denatured state of staphylococcal nuclease through the analysis of residual dipolar couplings./
Author:	Ackerman, Michael Scott, Jr.
Description:	92 p.
Notes:	Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4815.
Contained By:	Dissertation Abstracts International64-10B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3107469

Characterization of the long-range structure of the denatured state of staphylococcal nuclease through the analysis of residual dipolar couplings.
Ackerman, Michael Scott, Jr.

Characterization of the long-range structure of the denatured state of staphylococcal nuclease through the analysis of residual dipolar couplings. - 92 p.

Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4815.

Thesis (Ph.D.)--The Johns Hopkins University, 2004.

Structural analyses of denatured proteins have demonstrated that the polypeptide chain does not unfold to a random coil of featureless interactions. Previous work on a highly dynamic denatured fragment of staphylococcal nuclease, termed Delta131Subjects--Topical Terms:

1019105
Biophysics, General.

Characterization of the long-range structure of the denatured state of staphylococcal nuclease through the analysis of residual dipolar couplings.
LDR:01174nmm 2200265 4500 001 1862551
005 20041119083355.5
008 130614s2004 eng d
035 $a (UnM)AAI3107469
035 $a AAI3107469
040 $a UnM $c UnM
100 1 $a Ackerman, Michael Scott, Jr. $3 1950097
245 1 0 $a Characterization of the long-range structure of the denatured state of staphylococcal nuclease through the analysis of residual dipolar couplings.
300 $a 92 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4815.
500 $a Adviser: David Shortle.
502 $a Thesis (Ph.D.)--The Johns Hopkins University, 2004.
520 $a Structural analyses of denatured proteins have demonstrated that the polypeptide chain does not unfold to a random coil of featureless interactions. Previous work on a highly dynamic denatured fragment of staphylococcal nuclease, termed Delta131
590 $a School code: 0098.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0786
690 $a 0487
710 2 0 $a The Johns Hopkins University. $3 1017431
773 0 $t Dissertation Abstracts International $g 64-10B.
790 1 0 $a Shortle, David, $e advisor
790 $a 0098
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3107469