Differential scanning calorimetric and spectroscopic studies on the unfolding of Momordica charantia lectin. Similar modes of thermal and chemical denaturation

Calorimetric Study of Inulin as Cryo- and Lyoprotector of Bovine Plasma Proteins

“…It was found for all the saccharides that Td and H are scanning rate dependent. Td values increased 5  2 °C in all the samples with increasing scanning rate, similar behavior was reported in references [56][57][58]. Furthermore, the H decreased ( 10%) with increasing scanning rate that was in agreement with the results reported in references [21,59].…”

Structural basis for regulation of stability and activity in glyceraldehyde-3-phosphate dehydrogenases. Differential scanning calorimetry and molecular dynamics

“…The second peak seems to reflect a 650 highly cooperative denaturation of globular parts of the tetramers 651 whereas the first one corresponds to distortion of the quaternary 652 structure. The process of denaturation passed through two transi-653 tions was earlier detected for other tetramer proteins (Reddy et al,654 1999; Kavitha et al, 2010). These two transitions corresponded to 655 preliminary dissociation of the tetramers into monomers (Reddy 656 et al, 1999) or into dimers (Kavitha et al, 2010) and denaturation 657 of the latter.…”

“…The process of denaturation passed through two transi-653 tions was earlier detected for other tetramer proteins (Reddy et al,654 1999; Kavitha et al, 2010). These two transitions corresponded to 655 preliminary dissociation of the tetramers into monomers (Reddy 656 et al, 1999) or into dimers (Kavitha et al, 2010) and denaturation 657 of the latter. However the difference of the transition peaks tem-658 perature for those was about 10°C and the stages of denaturation 659 occurred one after another.…”

“…The component at 470 358 nm for GAPD from different sources relates to tryptophan pro-471 truded to intersubunit contacts and partly exposed to solvent. The The side chains of residues Arg126 (54) and Lys128 (56) (317) of denaturation for multi-subunit proteins (Makhatadze and 643 Privalov, 1995;Reddy et al, 1999;Kavitha et al, 2010). The curves 644 can be fitted by a sum of two Gaussian functions (Fig.…”

Assessment of interactions between four proteins and benzothiazole derivatives by DSC and CD

“…Physical and biological properties of a protein can be altered by conditions that affect its native conformation. The stability of a protein is generally estimated based on the analysis of its unfolding transitions induced by denaturants, such as urea, or by changes in the pH, ionic strength, or temperature, measured either spectroscopically or calorimetrically [16][17][18][19].…”