Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.

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Summary

A set of conformational restraints derived from nuclear magnetic resonance (n.m.r.) measurements on solutions of the basic pancreatic trypsin inhibitor (BPTI) was used as input for distance geometry calculations with the programs DISGEO and DISMAN and it is clear that the protein architecture observed in single crystals of BPTI is largely preserved in aqueous solution.

Type
article
Published
1987-08-05
Cited by
525
References
41

Keywords

Radius of gyration, Nuclear Overhauser effect, Geometry, Gyration, Crystallography

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