Trypsinogen-Trypsin Transition

Full molecular dynamics simulations of more than 1 ns are still almost prohibitive for large systems, so that a direct calculation of the relaxation time is difficult. However, it is possible to examine the flexibility of the activa- 

These results suggest that the N-terminal dipeptide is the trigger and that the glycine residues are the hinges for the trypsinogen-to-trypsin transition. Further work will be necessary to follow the dynamics of the transition and to estimate the entropic change involved in going from a disordered to an ordered structure. 

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Bode, W, R. Huber, Induction of the bovine trypsinogen-trypsin transition by peptides sequentially similar to the N-terminus of trypsin. FEBS Lett 1976, 68, 231-236. 

Disorder-to-order transition as part of enzyme activation (trypsinogen-trypsin)... 

Bode, W. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. J. Molec. Biol. 127, 357-402 (1979). 

Bode, W, P. Schwager, R. Huber, The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen— pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution. J Mol Biol 1978, 118, 99-112. 

Of particular significance are disorder-to-order transitions related to association part or aU of the polypeptide chain in one component is unfolded in the free form and becomes structured in the complex. We took the trypsin—PTI complex as an example of rigid-body association. The closely related trypsinogen—PTI complex is an example of a disorder-to-order transition. Its structure is essentially identical to that of trypsin— PTI, yet, in free trypsinogen, loops amounting to about one-quarter of the polypeptide chain are fuUy disordered. In the presence of PTI, they... 

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