Protein Disorder Flips Switch | Chemical & Engineering News
 
 
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Volume 91 Issue 25 | p. 31 | Concentrates
Issue Date: June 24, 2013

Protein Disorder Flips Switch

Availability of binding sites tunes signaling properties by switching between positive and negative cooperativity
Department: Science & Technology
News Channels: Biological SCENE

The binding of one molecule to a protein can affect subsequent binding of another molecule. That molecular response is known as allostery. Scientists already knew that intrinsic protein disorder—the lack of a defined structure—can modulate allosteric effects such as cooperativity. In positive cooperativity, binding of a molecule at one site increases binding of another molecule at a different site. Negative cooperativity decreases binding of the second molecule. Ashok A. Deniz,

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