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Cited by 163

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Racemic Protein Crystallography

Yeates, Todd O., Kent, Stephen B.H.·2012·Annual Review of Biophysics

Abstract

Although natural proteins are chiral and are all of one “handedness,” their mirror image forms can be prepared by chemical synthesis. This opens up new opportunities for protein crystallography. A racemic mixture of the enantiomeric forms of a protein molecule can crystallize in ways that natural proteins cannot. Recent experimental data support a theoretical prediction that this should make racemic protein mixtures highly amenable to crystallization. Crystals obtained from racemic mixtures also offer advantages in structure determination strategies. The relevance of these potential advantages is heightened by advances in synthetic methods, which are extending the size limit for proteins that can be prepared by chemical synthesis. Recent ideas and results in the area of racemic protein crystallography are reviewed.

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Metadata

Authors
Yeates, T. O., & Kent, S. B. H.
Venue
Annual Review of Biophysics
Published
2012-06-09
Volume
41
Issue
1
Pages
41-61
ISSN
  • 1936-122X (ISSN-L)
  • 1936-1238
OpenAlex
W2016024115
Cited by
163
References
1
FWCI
0.42
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Racemic Protein Crystallography. https://app.cochat.ai/papers/10.1146/annurev-biophys-050511-102333
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Yeates, T. O., & Kent, S. B. H. (2012). Racemic Protein Crystallography. Annual Review of Biophysics. https://doi.org/10.1146/annurev-biophys-050511-102333

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