Search for allosteric disulfide bonds in NMR structures.

ABSTRACT:

Background

Allosteric disulfide bonds regulate protein function when they break and/or form. They typically have a -RHStaple configuration, which is defined by the sign of the five chi angles that make up the disulfide bond.

Results

All disulfides in NMR and X-ray protein structures as well as in refined structure datasets were compared and contrasted for configuration and strain energy.

Conclusion

The mean dihedral strain energy of 55,005 NMR structure disulfides was twice that of 42,690 X-ray structure disulfides. Moreover, the energies of all twenty types of disulfide bond was higher in NMR structures than X-ray structures, where there was an exponential decrease in the mean strain energy as the incidence of the disulfide type increased. Evaluation of protein struc

SUBMITTER: Schmidt B 

PROVIDER: S-EPMC1949407 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature