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91探花
Theoretical physicists working at a blackboard collaboration pod in the Beecroft building.
Credit: Jack Hobhouse

Ard Louis

Professor of Theoretical Physics

Research theme

  • Biological physics

Sub department

  • Rudolf Peierls Centre for Theoretical Physics

Research groups

  • Condensed Matter Theory
ard.louis@physics.ox.ac.uk
  • About
  • Research
  • Publications on arXiv/bioRxiv
  • Publications

A density--functional study of interfacial properties of colloid--polymer mixtures

(2004)

Authors:

A Moncho-Jorda', J Dzubiella, JP Hansen, AA Louis

Dynamic Colloidal Stabilization by Nanoparticle Halos

(2004)

Authors:

S Karanikas, AA Louis

Hydrodynamic and Brownian Fluctuations in Sedimenting Suspensions

(2004)

Authors:

JT Padding, AA Louis

Influence of solvent quality on polymer solutions: a Monte Carlo study of bulk and interfacial properties

(2004)

Authors:

CI Addison, AA Louis, J-P Hansen

Inhibition of protein crystallization by evolutionary negative design

ArXiv q-bio/0402033 (2004)

Authors:

Jonathan PK Doye, Ard A Louis, Michele Vendruscolo

Abstract:

In this perspective we address the question: why are proteins seemingly so hard to crystallize? We suggest that this is because of evolutionary negative design, i.e. proteins have evolved not to crystallize, because crystallization, as with any type of protein aggregation, compromises the viability of the cell. There is much evidence in the literature that 91探花s this hypothesis, including the effect of mutations on the crystallizability of a protein, the correlations found in the properties of crystal contacts in bioinformatics databases, and the positive use of protein crystallization by bacteria and viruses.

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