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Biophysical Journal
Article
License: Elsevier Non-Commercial
Data sources: UnpayWall
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Biophysical Journal
Article . 2009
License: Elsevier Non-Commercial
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Biophysical Journal
Article . 2009 . Peer-reviewed
License: Elsevier Non-Commercial
Data sources: Crossref
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The Role Of Dynamics On Binding Specificity And Promiscuity

Authors: Ozkirimli, Elif; Keskin, Ozlem;

The Role Of Dynamics On Binding Specificity And Promiscuity

Abstract

Protein - protein interactions regulate and control a wide range of physiological processes. Protein interaction networks abound with proteins that have only a few connections while a small number of proteins, which are called hub proteins, are highly connected. Recent reports suggest that hub proteins are structurally and dynamically different from non-hub proteins. Hub proteins tend to be more disordered than other proteins. Further, binding partners of hub proteins are also observed to have higher levels of disorder. Here we perform a detailed examination of hub and non-hub proteins using the Gaussian Network Model (GNM) to elucidate the role of intrinsic dynamics for binding diversity and promiscuity.

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Biophysics

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
Average
Average
hybrid