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Principles and characteristics of biological assemblies in experimentally determined protein structures.

08:00 EDT 6th April 2019 | BioPortfolio

Summary of "Principles and characteristics of biological assemblies in experimentally determined protein structures."

More than half of all structures in the PDB are assemblies of two or more proteins, including both homooligomers and heterooligomers. Structural information on these assemblies comes from X-ray crystallography, NMR, and cryo-EM spectroscopy. The correct assembly in an X-ray structure is often ambiguous, and computational methods have been developed to identify the most likely biologically relevant assembly based on physical properties of assemblies and sequence conservation in interfaces. Taking advantage of the large number of structures now available, some of the most recent methods have relied on similarity of interfaces and assemblies across structures of homologous proteins.

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This article was published in the following journal.

Name: Current opinion in structural biology
ISSN: 1879-033X
Pages: 34-49

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