Proteins flex to function
NaturePublished 1 November 2005
Yuanpeng J. Huang, G.T. Montelione
Citations81
SJR quartileQ1
SJR score18.29
SNIP10.16
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Abstract
Static pictures of protein structures are so prevalent that it is easy to forget they are dynamic molecular machines. Characterizing their intrinsic motions may be necessary to understand how they work. Here's a new way to look at familiar enzymes. A new technology that can detect ultra-rare states of a protein (cyclophilin A in this instance) shows that rather than having a range of conformations to which it resorts during catalysis, it has them all before it starts. Protein motions needed for catalysis are intrinsic to the enzyme and take in the whole molecule, not just the traditional centre of attention, the active site.
Keywords
Materials ScienceBiochemistry, Genetics and Molecular Biology
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