The solution structure of human transforming growth factor α

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Abstract
The solution structure of transforming growth factor α has been determined by a combination of highresolution 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.