1ov2: Difference between revisions

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==Overview==

The 39 kDa receptor associated protein (RAP) is a modular protein, consisting of multiple domains. There has been no x-ray crystal structure, of RAP available and the full-length protein does not behave well in a NMR, tube. To elucidate the 3D structure of the RAP, we undertook structure, determination of individual domains of the RAP. As the first step, here we, report the nearly complete assignments of the (1)H, (13)C and (15)N, chemical shift signals of domain 1 of the RAP.

The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the (1)H, (13)C and (15)N chemical shift signals of domain 1 of the RAP.

==About this Structure==

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[[Category: Single protein]]

[[Category: Migliorini, M.]]

[[Category: Strickland, D.K.]]

[[Category: Strickland, D K.]]

[[Category: Wang, Y.X.]]

[[Category: Wang, Y X.]]

[[Category: Wu, Y.]]

[[Category: Yu, P.]]

[[Category: helical protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:51 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The 39 kDa receptor associated protein (RAP) is a modular protein, consisting of multiple domains. There has been no x-ray crystal structure, of RAP available and the full-length protein does not behave well in a NMR, tube. To elucidate the 3D structure of the RAP, we undertook structure, determination of individual domains of the RAP. As the first step, here we, report the nearly complete assignments of the (1)H, (13)C and (15)N, chemical shift signals of domain 1 of the RAP.
+The 39 kDa receptor associated protein (RAP) is a modular protein consisting of multiple domains. There has been no x-ray crystal structure of RAP available and the full-length protein does not behave well in a NMR tube. To elucidate the 3D structure of the RAP, we undertook structure determination of individual domains of the RAP. As the first step, here we report the nearly complete assignments of the (1)H, (13)C and (15)N chemical shift signals of domain 1 of the RAP.
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Migliorini, M.]]
-[[Category: Strickland, D.K.]]
+[[Category: Strickland, D K.]]
-[[Category: Wang, Y.X.]]
+[[Category: Wang, Y X.]]
 [[Category: Wu, Y.]]
 [[Category: Yu, P.]]
 [[Category: helical protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:36:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:51 2008''