Structure, stability, and dynamics of canonical and noncanonical base pairs: quantum chemical studies.

The importance of non-Watson-Crick base pairs in the three-dimensional structure of RNA is now well established. The structure and stability of these noncanonical base pairs are, however, poorly understood. We have attempted to understand structural features of 33 frequently occurring base pairs using density functional theory.

Conformational study of spectrin in presence of submolar concentrations of denaturants.

The presence of very low concentrations of the commonly used chemical denaturants, guanidinium chloride (GdmCl) and urea brought about conformational changes in the erythrocyte membrane skeletal protein, spectrin. Evidences in support of changes in the quaternary structure of spectrin have been put forward from quenching study of tryptophan fluorescence, by both steady state and time-resolved measurements, using acrylamide as the quencher. It revealed significant differences between the Stern-Volmer quenching constants (K(SV)) and the fraction of accessible tryptophans (f(e)) observed in absence and presence of GdmCl and urea concentrations below 1 M at which the association of the two subunits remains intact.

Effect of ionic strength on the organization and dynamics of tryptophan residues in erythroid spectrin: a fluorescence approach.

The ionic strength of the medium plays an important role in the structure and conformation of erythroid spectrin. The spectrin dimer is a flexible rod at physiological ionic strength. However, lower ionic strength results in elongation and rigidification (stiffening) of spectrin as shown earlier by electron microscopy and hydrodynamic studies.

Chaperone activity and prodan binding at the self-associating domain of erythroid spectrin.

Spectrin, the major constituent protein of the erythrocyte membrane skeleton, exhibits chaperone activity by preventing the irreversible aggregation of insulin at 25 degrees C and that of alcohol dehydrogenase at 50 degrees C. The dimeric spectrin and the two subunits, alpha-spectrin and beta-spectrin prevent such aggregation appreciably better, 70% in presence of dimeric spectrin at an insulin:spectrin ratio of 1:1, than that in presence of the tetramer of 25%. Our results also show that spectrin binds to denatured enzymes alpha-glucosidase and alkaline phosphatase during refolding and the reactivation yields are increased in the presence of the spectrin derivatives when compared with those refolded in their absence.