Isometrically invariant and allosterically aware description of deformable macromolecular surfaces: Application to the viral neuraminidase

Abstract Motivation: The macromolecular surfaces associated with proteins and macromolecules play a key role in determining their functionality and interactions, and are also of importance in structural analysis and classification. As a result of their interaction with their environment, the macromo...

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Bibliographic Details
Published in:Vaccine 2015-11, Vol.33 (48), p.6930-6937
Main Authors: Paquet, Eric, Viktor, Herna L
Format: Article
Language:English
Subjects:
Allergy and Immunology
Allosteric
Allosteric Regulation
Chemical Phenomena
Conflicts of interest
Deformable
Description
Euclidean space
Evolution
Fractional
Geometry
Heat kernel
Ligands
Macromolecular surface
Methods
Mutation
Neuraminidase
Neuraminidase - chemistry
Protein Conformation
Structural analysis
Surface Properties
Viral Proteins - chemistry
Citations: Items that this one cites
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Summary:Abstract Motivation: The macromolecular surfaces associated with proteins and macromolecules play a key role in determining their functionality and interactions, and are also of importance in structural analysis and classification. As a result of their interaction with their environment, the macromolecular surfaces experience random conformational deformations. Consequently, a realistic description of the molecular surface must be invariant under these deformations. Further, the motion associated with disconnected regions on the molecular surface may be correlated. This property is known as the allosteric effect. In this paper, we address these two requirements. To this end, we propose an approach based on discrete differential geometry and the fractional Fokker–Planck equation which provides an isometrically invariant and allosteric aware description of macromolecular surfaces. Our method is applied to the influenza neuraminidase.
ISSN:0264-410X
1873-2518
DOI:10.1016/j.vaccine.2015.08.098