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Default Demonstration of positionally disordered water within a protein hydrophobic cavity by
Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.

Related Articles Demonstration of positionally disordered water within a protein hydrophobic cavity by NMR.

Science. 1995 Mar 24;267(5205):1813-7

Authors: Ernst JA, Clubb RT, Zhou HX, Gronenborn AM, Clore GM

The presence and location of water of hydration (that is, bound water) in the solution structure of human interleukin-1 beta (hIL-1 beta) was investigated with water-selective two-dimensional heteronuclear magnetic resonance spectroscopy. It is shown here that in addition to water at the surface of the protein and ordered internal water molecules involved in bridging hydrogen bonds, positionally disordered water is present within a large, naturally occurring hydrophobic cavity located at the center of the molecule. These water molecules of hydration have residency times in the range of 1 to 2 nanoseconds to 100 to 200 microseconds and can be readily detected by nuclear magnetic resonance (NMR). Thus, large hydrophobic cavities in proteins may not be truly empty, as analysis of crystal structures appears to show, but may contain mobile water molecules that are crystallographically invisible but detectable by NMR.

PMID: 7892604 [PubMed - indexed for MEDLINE]



Source: PubMed
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