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Inhibition of protein crystallization by evolutionary negative design

dc.creatorDoye, Jonathan P. K.
dc.creatorLouis, Ard A.
dc.creatorVendruscolo, Michele
dc.date2004-02-16
dc.date.accessioned2026-06-02T21:40:47Z
dc.descriptionIn 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 supports 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.
dc.description5 pages
dc.identifierhttps://arxiv.org/abs/q-bio/0402033
dc.identifierhttp://arxiv.org/abs/q-bio/0402033
dc.identifierPhysical Biology 1, P9-P13 (2004)
dc.identifierdoi:10.1088/1478-3967/1/1/P02
dc.identifier.urihttps://demo.dspace.org/handle/10673/1674
dc.subjectBiomolecules
dc.subjectSoft Condensed Matter
dc.subjectBiological Physics
dc.titleInhibition of protein crystallization by evolutionary negative design
dc.typetext

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