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FEBS Letters|December 31, 1997
Effect of the chaperone-like alpha-crystallin on the refolding of lysozyme and ribonuclease AB Raman, T Ramakrishna, C M RaoFEBS Letters|May 29, 1995
Temperature dependent chaperone-like activity of alpha-crystallinB Raman, T Ramakrishna, C M RaoThe Journal of Biological Chemistry|August 25, 1995
Rapid refolding studies on the chaperone-like alpha-crystallin. Effect of alpha-crystallin on refolding of beta- and gamma-crystallinsB Raman, T Ramakrishna, C M RaoThe Journal of Biological Chemistry|July 19, 1996
Refolding of denatured and denatured/reduced lysozyme at high concentrationsB Raman, T Ramakrishna, C M RaoThe Biochemical Journal|October 24, 2001
Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivationS Goenka, B Raman, T Ramakrishna, et al.FEBS Letters|May 30, 2001
Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturationK Rajaraman, B Raman, T Ramakrishna, et al.Biochemical and Biophysical Research Communications|September 10, 1998
The chaperone-like alpha-crystallin forms a complex only with the aggregation-prone molten globule state of alpha-lactalbuminK Rajaraman, B Raman, T Ramakrishna, et al.FEBS Letters|January 15, 1998
Co-refolding denatured-reduced hen egg white lysozyme with acidic and basic proteinsV D Trivedi, B Raman, C M Rao, et al.Journal of Biochemical and Biophysical Methods|September 11, 1999
Detection and assay of proteases using calf lens beta-crystallin aggregate as substrateV D Trivedi, B Raman, T Ramakrishna, et al.The Journal of Biological Chemistry|November 4, 1994
Chaperone-like activity and quaternary structure of alpha-crystallinB Raman, C M RaoPageof 13