V. M. Tischenko

TL;DR: The thermodynamic analysis of microcalorimetric and hydrogen exchange data on the stability and mobility of collagen structures from different species with different physiological temperatures has shown that not only the thermostability but the enthalpy and entropy of disruption of the native collagen structure are increasing functions of the total prolyl and hydroxyprolyl content as mentioned in this paper.

TL;DR: The X-ray structure for a native chaperone-fibre complex shows that the final folding step is indeed an essential component of the assembly process, and shows that completion of the hydrophobic core and incorporation into the fibre results in an exceptionally stable module, whereas the chaper one-subunit pre-assembly complex is greatly destabilized by the high-energy conformation of the bound subunit.

TL;DR: The intramolecular melting of rabbit immunoglobulin G and its proteolytic fragments has been studied by scanning microcalorimetry in the acidic pH region and by thermodynamic analysis of the heat capacity function the following conclusions are made.

TL;DR: It may be postulated that the conservative part of CH2 domains makes a cardinal contribution to the interaction of these domains with the carbohydrate moiety.

TL;DR: Structural analysis of the human immunoglobulin G (hIgG2) revealed two types of interaction between CH1 domain of Fab (antigen-binding fragment/ subunit) and CH2 domain of Fc (complement fixation fragment/subunit) simultaneously present in the sample, which should lead to better design of antibody-based therapeutics.