2blg
From Proteopedia
(New page: 200px<br /><applet load="2blg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2blg, resolution 2.46Å" /> '''STRUCTURAL BASIS OF ...) |
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| - | [[Image:2blg.gif|left|200px]]<br /><applet load="2blg" size=" | + | [[Image:2blg.gif|left|200px]]<br /><applet load="2blg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2blg, resolution 2.46Å" /> | caption="2blg, resolution 2.46Å" /> | ||
'''STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2'''<br /> | '''STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structures of the trigonal crystal form of bovine beta-lactoglobulin | + | The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition. |
==About this Structure== | ==About this Structure== | ||
| - | 2BLG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http:// | + | 2BLG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BLG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Baker, E | + | [[Category: Baker, E N.]] |
| - | [[Category: Baker, H | + | [[Category: Baker, H M.]] |
| - | [[Category: Bewley, M | + | [[Category: Bewley, M C.]] |
| - | [[Category: Creamer, L | + | [[Category: Creamer, L K.]] |
| - | [[Category: Jameson, G | + | [[Category: Jameson, G B.]] |
| - | [[Category: Qin, B | + | [[Category: Qin, B Y.]] |
[[Category: beta-lactoglobulin]] | [[Category: beta-lactoglobulin]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:03 2008'' |
Revision as of 14:39, 21 February 2008
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STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2
Overview
The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.
About this Structure
2BLG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis of the Tanford transition of bovine beta-lactoglobulin., Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB, Biochemistry. 1998 Oct 6;37(40):14014-23. PMID:9760236
Page seeded by OCA on Thu Feb 21 16:39:03 2008
