Refolding by disulfide isomerization - the mixed disulfide between ribonuclease t-1 and glutathione as a model refolding...
... was studied using the mixed disulfide between glutathione and reduced ribonuclease T-1 (GS-RNase T-1) as a stable soluble and ... appearance of native ribonuclease activity, HPLC, and nonreducing SDS-PAGE, All the analyses indicated that native RNase T-1 ... GS-RNase T-1 refolding was inhibited by BiP; refolding was completely blocked in presence of a 5-fold molar excess of BiP, and ... In 1.5 M NaCl, GS-RNase T-1 adopts a compact native-like conformation; refolding by thiol-disulfide interchange in these ...https://kar.kent.ac.uk/19005/
Items where Subject is "Q Science | QP Physiology (Living systems) | QP517 Biochemistry" - Kent Academic Repository
Freedman, Robert B. and Ruoppolo, Margherita (1995) Refolding of the mixed Disulfide of Rnase T-1 and Glutathione. In: 652nd ... Early intermediates in the PDI-assisted folding of ribonuclease A. Protein Science, 9 (3). pp. 525-535. ISSN 0961-8368. (The ...https://kar.kent.ac.uk/view/subjects/QP517.html
Items where division is "Faculties | Sciences | School of Biosciences | Protein Science Group" - Kent Academic Repository
Schmidt, Jürgen M. and Löhr, Frank (2012) 3J coupling constants related to the phi-torsion angles in Ribonuclease T1 (EC 3.1. ... Schmidt, Jürgen M. and Löhr, Frank (2008) 1J coupling constants related to the Ca carbons in Ribonuclease T1 from Aspergillus ... Schmidt, Jürgen M. and Löhr, Frank (2010) 2J coupling constants in Ribonuclease T1 from Aspergillus oryzae. Biological Magnetic ...https://kar.kent.ac.uk/view/divisions/12100=2F1.default.html
Protein-S-S-Glutathione Mixed Disulfides as Models of Unfolded Protein - Kent Academic Repository
RNase T-1 and alpha-lactalbumin were reduced and converted to mixed disulfide derivatives, named GS-RNase T-1 and GS-alpha- ... Fluorescence studies and enzyme activity data indicated that GS-RNase T-1 could be refolded to a nativelike state at NaCl ... The [NaCl]-dependent folding/unfolding equilibrium for GS-RNase T-1 was reversible and could be influenced by urea. ...https://kar.kent.ac.uk/20008/