Structural studies on lens proteins

Structural Studies on Cytoskeletal Proteins.

A number of componenets of cytoskeleton are very large proteins which are in their complete native form non amenable to the structure determination via X-ray diffraction techniques due to their non-globular shape and intrinsic flexibility which hinder the formation of suitable crystals. Dissecting such proteins into their representative building blocks-domains and subsequent structural studies ...

Structural studies on lysosomal proteins

Studies on lens proteins. I. Subunit structure of beta crystallins of rabbit lens cortex.

A method has been developed to isolate and characterize beta-crystallins of rabbit lens cortex. Chromatographic separation of water-soluble structure proteins of rabbit lens cortex on a Sephacryl S-200 gel column yielded four beta-crystallin peaks (beta1, beta2, beta3 and beta4), all eluting between alpha and gamma-crystallins. Their molecular weights were estimated to be 250,000, 130,000, 60,0...

Studies on lens proteins. III. Variations in polypeptides of lens beta-crystallins.

Relative amounts of two water-soluble beta-crystallin polypeptides with molecular weights of 26,000 (26K) and 28,000 daltons (28K) were measured in a number of species and also in different age groups of rats. The data indicate an age-dependent increase in the quantity of the 26K which is concomitant with a decrease in the 28K polypeptide. The ratio of these two polypeptides in the total water-...

Studies on the lens.