2tgf
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The solution structure of transforming growth factor alpha has been | + | The solution structure of transforming growth factor alpha has been determined by a combination of high-resolution 1H-nuclear magnetic resonance and distance geometry and restrained molecular dynamics. The 382 restraints derived from the NMR experiments were used to calculate many distance geometry structures, which were then refined by restrained molecular mechanics. Five of these structures were further refined using a variety of methods. Comparison of independently measured parameters, such as calculated hydrogen bonding patterns and experimental amide exchange rates, have been used to evaluate the accuracy of the structures. Also, possible mechanisms to explain the pH-dependent conformational interconversion observed are suggested. Finally comparisons between this work and others on this topic have been made. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Campbell, I | + | [[Category: Campbell, I D.]] |
| - | [[Category: Cooke, R | + | [[Category: Cooke, R M.]] |
| - | [[Category: Harvey, T | + | [[Category: Harvey, T S.]] |
| - | [[Category: Tappin, M | + | [[Category: Tappin, M J.]] |
| - | [[Category: Wilkinson, A | + | [[Category: Wilkinson, A J.]] |
[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:41 2008'' |
Revision as of 16:49, 21 February 2008
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THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA
Overview
The solution structure of transforming growth factor alpha has been determined by a combination of high-resolution 1H-nuclear magnetic resonance and distance geometry and restrained molecular dynamics. The 382 restraints derived from the NMR experiments were used to calculate many distance geometry structures, which were then refined by restrained molecular mechanics. Five of these structures were further refined using a variety of methods. Comparison of independently measured parameters, such as calculated hydrogen bonding patterns and experimental amide exchange rates, have been used to evaluate the accuracy of the structures. Also, possible mechanisms to explain the pH-dependent conformational interconversion observed are suggested. Finally comparisons between this work and others on this topic have been made.
About this Structure
2TGF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The solution structure of human transforming growth factor alpha., Harvey TS, Wilkinson AJ, Tappin MJ, Cooke RM, Campbell ID, Eur J Biochem. 1991 Jun 15;198(3):555-62. PMID:2050136
Page seeded by OCA on Thu Feb 21 18:49:41 2008
