The solution structure of human transforming growth factor alpha.
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.
Harvey
T S
TS
Department of Biochemistry, University of Oxford, England.
Wilkinson
A J
AJ
Tappin
M J
MJ
Cooke
R M
RM
Campbell
I D
ID
D000595:Amino Acid Sequence; D006801:Humans; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012996:Solutions; D016211:Transforming Growth Factor alpha / Q000737:chemistry*
D012996:Solutions; D016211:Transforming Growth Factor alpha