Epistructural Tension Promotes Protein Associations - sprookjes - yvandenbroek - TriplyDB

Epistructural Tension Promotes Protein Associations

Epistructural Tension Promotes Protein Associations

http://www.wikidata.org/entity/Q21563730

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Heterogeneous preferential solvation of water and trifluoroethanol in homologous lysozymes.Viscoelasticity and shear thinning of nanoconfined water.The principle of minimal episteric distortion of the water matrix and its steering role in protein folding.Breakdown of the Debye polarization ansatz at protein-water interfaces.Communication: Nanoscale electrostatic theory of epistructural fields at the protein-water interface.Long-range interlayer alignment of intralayer domains in stacked lipid bilayers.Acid-base chemistry of frustrated water at protein interfaces.Dielectric response of frustrated water down to a single-molecule contribution Catalytic Role of Dehydrons in Soluble Proteins: Biological Chemistry of Frustrated Interfacial Water Dielectric Structure of Aqueous Interfaces: From Classical Non-Debye Electrostatics to a Quantum Theory of Interfacial Tension Interfacial Physics for Water in Biology Structure-Based Drug Discovery Without Structure: Working Around the Paradox to Disrupt Protein-Protein Associations Communication: Chemical functionality of interfacial water enveloping nanoscale structural defects in proteins

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Epistructural Tension Promotes Protein Associations

http://www.wikidata.org/entity/Q21563730

description

2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Epistructural Tension Promotes Protein Associations

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Epistructural Tension Promotes Protein Associations

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PHYSREVLETT.108.188102

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Physical Review Letters

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Epistructural Tension Promotes Protein Associations

@en

P2860

Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes

A simple physical model for binding energy hot spots in protein-protein complexes

A hot spot of binding energy in a hormone-receptor interface

Unraveling hot spots in binding interfaces: progress and challenges

Mapping the CD4 binding site for human immunodeficiency virus by alanine-scanning mutagenesis.

Entropy and the driving force for the filling of carbon nanotubes with water.

Site-specific mutagenesis reveals differences in the structural bases for tight binding of RNase inhibitor to angiogenin and RNase A.

Biological water: Its vital role in macromolecular structure and function.

Hydrophobicity of protein surfaces: Separating geometry from chemistry

Molecular characterization of the hdm2-p53 interaction.

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188102

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scholarly article

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10.1103/PHYSREVLETT.108.188102

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18

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108

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Ariel Fernández

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2012-05-01T00:00:00Z

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22681121

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