1bcu: Difference between revisions

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==Overview==

Proflavin can be used to study the interactions of inhibitors and, substrates with thrombin by monitoring the changes in the visible, absorption spectrum that occur on dye displacement. We have used, microspectrophotometric methods to investigate the binding of proflavin to, crystals of an alpha-thrombin-hirugen complex and have determined the, structure by X-ray crystallography. The proflavin molecule binds in the S1, pocket of the enzyme with one of the amino groups hydrogen bonded to the, carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen, bonded to the carbonyl of Gly-219. This result indicates that the, proflavin displacement assay can be used to specifically monitor the, binding of inhibitors to the S1 pocket.

Proflavin can be used to study the interactions of inhibitors and substrates with thrombin by monitoring the changes in the visible absorption spectrum that occur on dye displacement. We have used microspectrophotometric methods to investigate the binding of proflavin to crystals of an alpha-thrombin-hirugen complex and have determined the structure by X-ray crystallography. The proflavin molecule binds in the S1 pocket of the enzyme with one of the amino groups hydrogen bonded to the carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen bonded to the carbonyl of Gly-219. This result indicates that the proflavin displacement assay can be used to specifically monitor the binding of inhibitors to the S1 pocket.

==Disease==

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[[Category: serine protease]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:31:49 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:04 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Proflavin can be used to study the interactions of inhibitors and, substrates with thrombin by monitoring the changes in the visible, absorption spectrum that occur on dye displacement. We have used, microspectrophotometric methods to investigate the binding of proflavin to, crystals of an alpha-thrombin-hirugen complex and have determined the, structure by X-ray crystallography. The proflavin molecule binds in the S1, pocket of the enzyme with one of the amino groups hydrogen bonded to the, carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen, bonded to the carbonyl of Gly-219. This result indicates that the, proflavin displacement assay can be used to specifically monitor the, binding of inhibitors to the S1 pocket.
+Proflavin can be used to study the interactions of inhibitors and substrates with thrombin by monitoring the changes in the visible absorption spectrum that occur on dye displacement. We have used microspectrophotometric methods to investigate the binding of proflavin to crystals of an alpha-thrombin-hirugen complex and have determined the structure by X-ray crystallography. The proflavin molecule binds in the S1 pocket of the enzyme with one of the amino groups hydrogen bonded to the carboxylate of Asp-189 while the protonated ring nitrogen is hydrogen bonded to the carbonyl of Gly-219. This result indicates that the proflavin displacement assay can be used to specifically monitor the binding of inhibitors to the S1 pocket.
 ==Disease==
@@ Line 27: / Line 27: @@
 [[Category: serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:31:49 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:04 2008''