β-Crystallins, the oligomeric proteins of the eye lens, were found to bind calcium ions with low affinity, in the millimolar range. Calcium was found to induce conformational changes in the secondary and tertiary structure of β-crystallins. While these changes in conformation are seen in low ionic strength media, they are masked when the protein is dissolved in an intermediate ionic strength medium, where oligomers of lower molecular weight are formed. The calcium binding takes place in these conditions. The behaviour of this protein with respect to calcium binding is reviewed
Using spectroscopic, calorimetric and microscopic methods, we demonstrate that calcium binds to beta...
Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 9311, Acharya Prafulla Chandr...
Using spectroscopic, calorimetric and microscopic methods, we demonstrate that calcium binds to beta...
The β- and γ-crystallins are closely related lens proteins that are members of the βγ-crystallin sup...
The β- and γ-crystallins are closely related lens proteins that are members of the βγ-crystallin sup...
Abnormal levels of endogenous calcium ions are known to induce eye lens opacity, and a variety of ca...
β-crystallin, one of the three main constituent proteins of the eye lens, exists as an equilibrium p...
βγ-crystallins are structural proteins in the eye lens that refract light to produce an image. These...
The tunicate (Ciona intestinalis) βγ-crystallin represents an intermediate case between the calcium-...
The interaction of the cationic carbocyanine dye Stains-all (1-ethyl-2-[3-(1-ethyl-naphthol[1,2-d]th...
βγ-Crystallin is a superfamily with diverse members from vertebrate lens to microbes. However, not m...
This thesis examines the biophysical properties of beta/gamma-crystallin proteins with a specific fo...
The interaction of the cationic carbocyanine dye Stains-all (1-ethyl-2-[3-(1-ethyl-naphthol[1,2-d]th...
The βγ-crystallin superfamily consists of evolutionarily related proteins with domain topology simil...
Crystallins are water-soluble proteins that are necessary for focusing light on the retina. In mamma...
Using spectroscopic, calorimetric and microscopic methods, we demonstrate that calcium binds to beta...
Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 9311, Acharya Prafulla Chandr...
Using spectroscopic, calorimetric and microscopic methods, we demonstrate that calcium binds to beta...
The β- and γ-crystallins are closely related lens proteins that are members of the βγ-crystallin sup...
The β- and γ-crystallins are closely related lens proteins that are members of the βγ-crystallin sup...
Abnormal levels of endogenous calcium ions are known to induce eye lens opacity, and a variety of ca...
β-crystallin, one of the three main constituent proteins of the eye lens, exists as an equilibrium p...
βγ-crystallins are structural proteins in the eye lens that refract light to produce an image. These...
The tunicate (Ciona intestinalis) βγ-crystallin represents an intermediate case between the calcium-...
The interaction of the cationic carbocyanine dye Stains-all (1-ethyl-2-[3-(1-ethyl-naphthol[1,2-d]th...
βγ-Crystallin is a superfamily with diverse members from vertebrate lens to microbes. However, not m...
This thesis examines the biophysical properties of beta/gamma-crystallin proteins with a specific fo...
The interaction of the cationic carbocyanine dye Stains-all (1-ethyl-2-[3-(1-ethyl-naphthol[1,2-d]th...
The βγ-crystallin superfamily consists of evolutionarily related proteins with domain topology simil...
Crystallins are water-soluble proteins that are necessary for focusing light on the retina. In mamma...
Using spectroscopic, calorimetric and microscopic methods, we demonstrate that calcium binds to beta...
Protein Chemistry Laboratory, Department of Chemistry, Bose Institute, 9311, Acharya Prafulla Chandr...
Using spectroscopic, calorimetric and microscopic methods, we demonstrate that calcium binds to beta...