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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

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.

Inhibition of protein crystallization by evolutionary negative design

(2004)

Authors:

Jonathan PK Doye, Ard A Louis, Michele Vendruscolo

Hydrodynamic and Brownian fluctuations in sedimenting suspensions

PHYSICAL REVIEW LETTERS 93:22 (2004) ARTN 220601

Authors:

JT Padding, AA Louis

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

JOURNAL OF CHEMICAL PHYSICS 121:1 (2004) 612-620

Authors:

CI Addison, AA Louis, JP Hansen

Phase separation of a multiple occupancy lattice gas

JOURNAL OF PHYSICS A-MATHEMATICAL AND GENERAL 37:3 (2004) PII S0305-4470(04)70238-3

Authors:

R Finken, JP Hansen, AA Louis

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