dorsal/arxiv
View SchemaInhibition of protein crystallization by evolutionary negative design
| Authors | Jonathan P. K. Doye, Ard A. Louis, Michele Vendruscolo |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0402033 |
| URL | https://arxiv.org/abs/q-bio/0402033 |
| DOI | 10.1088/1478-3967/1/1/P02 |
| Journal | Physical Biology 1, P9-P13 (2004) |
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 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.
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"abstract": "In this perspective we address the question: why are proteins seemingly so\nhard to crystallize? We suggest that this is because of evolutionary negative\ndesign, i.e. proteins have evolved not to crystallize, because crystallization,\nas with any type of protein aggregation, compromises the viability of the cell.\nThere is much evidence in the literature that supports this hypothesis,\nincluding the effect of mutations on the crystallizability of a protein, the\ncorrelations found in the properties of crystal contacts in bioinformatics\ndatabases, and the positive use of protein crystallization by bacteria and\nviruses.",
"arxiv_id": "q-bio/0402033",
"authors": [
"Jonathan P. K. Doye",
"Ard A. Louis",
"Michele Vendruscolo"
],
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"q-bio.BM",
"cond-mat.soft",
"physics.bio-ph"
],
"doi": "10.1088/1478-3967/1/1/P02",
"journal_ref": "Physical Biology 1, P9-P13 (2004)",
"title": "Inhibition of protein crystallization by evolutionary negative design",
"url": "https://arxiv.org/abs/q-bio/0402033"
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