東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

The thermodynamic linkage of proton ...

Negin, Russell Scott.

FindBook

Google Book

Amazon

博客來

The thermodynamic linkage of proton binding and protein function.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	The thermodynamic linkage of proton binding and protein function./
作者:	Negin, Russell Scott.
面頁冊數:	212 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-05, Section: B, page: 2081.
Contained By:	Dissertation Abstracts International64-05B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3089879
ISBN:	0496376045

The thermodynamic linkage of proton binding and protein function.
Negin, Russell Scott.

The thermodynamic linkage of proton binding and protein function. - 212 p.

Source: Dissertation Abstracts International, Volume: 64-05, Section: B, page: 2081.

Thesis (Ph.D.)--Princeton University, 2003.

This thesis describes the development and use of new experimental tools and computational techniques to assess the role of interactions between charged groups on the stability and activity of proteins. This stability and activity are quantitatively indicated by changes in free energy as a result of protein folding and ligand binding, respectively. The techniques of capillary electrophoresis (CE) and charge ladders measure the linkage between the cooperativity of proton binding and protein function. Monte Carlo simulations together with Poisson Boltzmann theory of continuum electrostatics are used to model this thermodynamic linkage. The combination of experiments and modeling provides general design principles for the effective engineering of proteins via interactions between charged groups.

ISBN: 0496376045Subjects--Topical Terms:

1019105
Biophysics, General.

The thermodynamic linkage of proton binding and protein function.
LDR:03120nmm 2200313 4500 001 1837484
005 20050506072705.5
008 130614s2003 eng d
020 $a 0496376045
035 $a (UnM)AAI3089879
035 $a AAI3089879
040 $a UnM $c UnM
100 1 $a Negin, Russell Scott. $3 1925932
245 1 4 $a The thermodynamic linkage of proton binding and protein function.
300 $a 212 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-05, Section: B, page: 2081.
500 $a Adviser: Jeffrey Carbeck.
502 $a Thesis (Ph.D.)--Princeton University, 2003.
520 $a This thesis describes the development and use of new experimental tools and computational techniques to assess the role of interactions between charged groups on the stability and activity of proteins. This stability and activity are quantitatively indicated by changes in free energy as a result of protein folding and ligand binding, respectively. The techniques of capillary electrophoresis (CE) and charge ladders measure the linkage between the cooperativity of proton binding and protein function. Monte Carlo simulations together with Poisson Boltzmann theory of continuum electrostatics are used to model this thermodynamic linkage. The combination of experiments and modeling provides general design principles for the effective engineering of proteins via interactions between charged groups.
520 $a The results of the experimental and computational work are consistent. In both protein folding and binding, relying on a single protonation state may not capture all of the physics occurring throughout the processes. Experimental studies on alpha-lactalbumin show a strong change in protonation state as a result of denaturation. Computational studies on barnase and barstar also reveal a change in the protonation states of barnase and barstar upon binding; this change is modeled accurately by allowing the observed protonation states to be averages of many protonation states in equilibrium. Thus, the observed change in protonation state is in reality a change in the distribution of ensembles of protonation states.
520 $a This thesis is intended to give the reader an idea of the significance with which the extent of cooperativity of proton binding can affect the structure and activity of a protein molecule. Since electrostatic interactions are long range, modifying a single site can affect many other titratable groups in the protein resulting in a large collective energetic impact. The consequences of this thesis are a starting point for the scientist to regulate cooperativity of a protein so that by modifying a few key residues, one can engineer protein function and stability without significantly altering the surface potential on the protein or the protein chemical composition.
590 $a School code: 0181.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Engineering, Chemical. $3 1018531
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0786
690 $a 0542
690 $a 0487
710 2 0 $a Princeton University. $3 645579
773 0 $t Dissertation Abstracts International $g 64-05B.
790 1 0 $a Carbeck, Jeffrey, $e advisor
790 $a 0181
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3089879