2b75
From Proteopedia
Line 1: | Line 1: | ||
[[Image:2b75.gif|left|200px]] | [[Image:2b75.gif|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_2b75", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_2b75| PDB=2b75 | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''T4 Lysozyme mutant L99A at 150 MPa''' | '''T4 Lysozyme mutant L99A at 150 MPa''' | ||
Line 30: | Line 27: | ||
[[Category: Matthews, B W.]] | [[Category: Matthews, B W.]] | ||
[[Category: Quillin, M L.]] | [[Category: Quillin, M L.]] | ||
- | [[Category: | + | [[Category: Cavity]] |
- | [[Category: | + | [[Category: High pressure]] |
- | [[Category: | + | [[Category: T4 lysozyme]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:56:13 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 16:56, 3 May 2008
T4 Lysozyme mutant L99A at 150 MPa
Overview
Formation of a water-expelling nonpolar core is the paradigm of protein folding and stability. Although experiment largely confirms this picture, water buried in "hydrophobic" cavities is required for the function of some proteins. Hydration of the protein core has also been suggested as the mechanism of pressure-induced unfolding. We therefore are led to ask whether even the most nonpolar protein core is truly hydrophobic (i.e., water-repelling). To answer this question we probed the hydration of an approximately 160-A(3), highly hydrophobic cavity created by mutation in T4 lysozyme by using high-pressure crystallography and molecular dynamics simulation. We show that application of modest pressure causes approximately four water molecules to enter the cavity while the protein itself remains essentially unchanged. The highly cooperative filling is primarily due to a small change in bulk water activity, which implies that changing solvent conditions or, equivalently, cavity polarity can dramatically affect interior hydration of proteins and thereby influence both protein activity and folding.
About this Structure
2B75 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation., Collins MD, Hummer G, Quillin ML, Matthews BW, Gruner SM, Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16668-71. Epub 2005 Nov 3. PMID:16269539 Page seeded by OCA on Sat May 3 19:56:13 2008