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Modeling of protein interactions in ...

Asthagiri, Dilipkumar N.

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Modeling of protein interactions in solution.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Modeling of protein interactions in solution./
Author:	Asthagiri, Dilipkumar N.
Description:	200 p.
Notes:	Professor in charge: Abraham M. Lenhoff.
Contained By:	Dissertation Abstracts International60-08B.
Subject:	Biophysics, General. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9941007
ISBN:	9780599425354

Modeling of protein interactions in solution.
Asthagiri, Dilipkumar N.

Modeling of protein interactions in solution. - 200 p.

Professor in charge: Abraham M. Lenhoff.

Thesis (Ph.D.)--University of Delaware, 1999.

Interactions involving proteins are central to many in vivo and in vitro processes. This work is an endeavor to understand the physical aspects of these interactions in quantitative and qualitative terms by decomposing them into protein-surface, protein-ligand and protein-protein interactions.

ISBN: 9780599425354Subjects--Topical Terms:

1019105
Biophysics, General.

Modeling of protein interactions in solution.
LDR:03561nam 2200349 a 45 001 970740
005 20110921
008 110921s1999 eng d
020 $a 9780599425354
035 $a (UMI)AAI9941007
035 $a AAI9941007
040 $a UMI $c UMI
100 1 $a Asthagiri, Dilipkumar N. $3 1294785
245 1 0 $a Modeling of protein interactions in solution.
300 $a 200 p.
500 $a Professor in charge: Abraham M. Lenhoff.
500 $a Source: Dissertation Abstracts International, Volume: 60-08, Section: B, page: 4086.
502 $a Thesis (Ph.D.)--University of Delaware, 1999.
520 $a Interactions involving proteins are central to many in vivo and in vitro processes. This work is an endeavor to understand the physical aspects of these interactions in quantitative and qualitative terms by decomposing them into protein-surface, protein-ligand and protein-protein interactions.
520 $a To explore the sensitivity to assumed structural details in protein-surface interactions, we have modeled an anomalous adsorption process involving a net positively charged protein adsorbing onto a positively charged surface. This study reveals the importance of accounting for the discreteness of charge on the adsorbent surface.
520 $a The specificity of protein-ligand interactions is considered in calculations of acetate and methyl sulfate ligands interacting with the protein and with methyl ammonium. The results reveal the inability of continuum models to discriminate fine differences in interaction, which are attributable mainly to the local solvent structure and associated polarization effects. To describe these effects more effectively, we suggest a possible method that treats the local environment quantum mechanically and the rest of the system as a continuum.
520 $a Investigations of protein-protein interactions in solution reveal that biological specificity is observable in measured thermodynamic properties. Specifically, it is seen that the osmotic second virial coefficient is most strongly affected by a small number of high-complementarity configurations, which are also seen in crystal contacts. We are thus able to explain the empirically observed correlation between the second virial coefficient and the propensity for protein solution to form crystals.
520 $a Our investigation of protein incorporation into a crystal phase suggests that molecules with configurations incommensurate with the crystal symmetry can act as competitive inhibitors of crystal growth. The rate of crystal growth thus depends on the changes in specificity of the commensurate orientation vis a vis those of the incommensurate orientations for the crystal face. Thus procedures aimed at decreasing the effect of such competitive inhibition are expected to offer better control of crystal growth rates.
520 $a The modeling of protein interactions has thus revealed nuances of these interactions that were hitherto either unknown or only poorly understood. We now possess a much better understanding of the dominant physical effects involving proteins in various scenarios, and such knowledge will prove invaluable in advancing towards building a functional picture of a protein in solution and of functioning organisms.
590 $a School code: 0060.
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Physical. $3 560527
650 4 $a Engineering, Chemical. $3 1018531
690 $a 0494
690 $a 0542
690 $a 0786
710 2 0 $a University of Delaware. $3 1017826
773 0 $t Dissertation Abstracts International $g 60-08B.
790 $a 0060
790 1 0 $a Lenhoff, Abraham M., $e advisor
791 $a Ph.D.
792 $a 1999
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9941007