This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1u06

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1u06.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1u06.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u06| PDB=1u06 | SCENE= }}
{{STRUCTURE_1u06| PDB=1u06 | SCENE= }}
-
'''crystal structure of chicken alpha-spectrin SH3 domain'''
+
===crystal structure of chicken alpha-spectrin SH3 domain===
-
==Overview==
+
<!--
-
Water molecules are a major determinant of protein stability and are important for understanding protein-protein interactions. We present two experiments which allow to measure first the effective T(2) decay rate of individual amide proton, and second the magnetization build-up rates for a selective transfer from H(2)O to H(N) using spin diffusion as a mixing element. The experiments are demonstrated for a uniformly (2)H, (15)N labeled sample of a microcrystalline SH3 domain in which exchangeable deuterons were back-substituted with protons. In order to evaluate the NMR experimental data, as X-ray structure of the protein was determined using the same crystallization protocol as for the solid-state NMR sample. The NMR experimental data are correlated with the dipolar couplings calculated from H(2)O-H(N) distances which were extracted from the X-ray structure of the protein. We find that the H(N) T(2) decay rates and H(2)O-H(N) build-up rates are sensitive to distance and dynamics of the detected water molecules with respect to the protein. We show that qualitative information about localization and dynamics of internal water molecules can be obtained in the solid-state by interpretation of the spin dynamics of a reporter amide proton.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15928996}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15928996 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15928996}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Five antiparallel beta sheet]]
[[Category: Five antiparallel beta sheet]]
[[Category: Sh3 domain]]
[[Category: Sh3 domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:34:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 6 00:57:08 2008''

Revision as of 21:57, 5 July 2008

Image:1u06.png

Template:STRUCTURE 1u06

crystal structure of chicken alpha-spectrin SH3 domain

Template:ABSTRACT PUBMED 15928996

About this Structure

1U06 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR., Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B, J Biomol NMR. 2005 Apr;31(4):295-310. PMID:15928996

Page seeded by OCA on Sun Jul 6 00:57:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u06"
Personal tools