Detection of conformation changes of proteins through the changes in rate constants of cooperative proteolysisBiochemistry > Amino Acids and Peptides and Proteinsbiochem/0105002The changes in the egg lysozyme and soybean glycinin conformation under the action of increasing urea concentration were followed ...
Based on the simulations, we analyzed the conformation changes of Aβ42 protein and the formation of its secondary structure and tertiary structure. The results indicated that Aβ42 protein has no stable structure and it has the characters of intrinsically disorder proteins at the different ...
A model to describe the mechanism of conformational dynamics in protein based on matter interactions using lagrangian approach and imposing certain symmetry breaking is proposed. Both conformation changes of proteins and the injected non-linear sources are represented by the bosonic lagrangian with an add...
A fluorometric technique is described for the study of conformational changes in proteins covalently bound to insoluble carriers. The fluorescence peak of chymotrypsin bound to cyanogen bromide activated Sephadex or agarose shifted to the red in the presence of 8 M urea, similarly to chymotrypsin in ...
Raman spectroscopy was employed to monitor the structural changes of proteins during gelling, and intermolecular bonding as a function of temperature was measured. Pre-incubation at 40 °C significantly increased the breaking force of the cooked fish sample, but had little effect on the breaking ...
The Role of Heat-Shock Proteins in Thermotolerance [and Discussion] Aggregates found in mutant cells at high temperatures suggest that the cause of death may be the accumulation of denatured proteins. No differences in the... DA Parsell,J Taulien,S Lindquist,... - 《Philosophical Transactions...
Molecular conformation is any spatial arrangement of the atoms in a molecule which can be interconverted by rotations about formally single bonds. Biopolymers, such as polynucleotides, polypeptides or polysaccharides, may change conformation in response to changes in their environment. Latest Research ...
To see how open and closed forms are quantitively different each other, we analysed the inter-domain rotation of GHRC in Uso1GHR using DynDom program21, which analyses conformational changes in proteins containing hinge-bending regions. In this analysis, the fixed domains were defined as residues...
Thus, the absorption changes observed near 230 mµ for globular proteins result primarily from changes in the environment of the aromatic chromophores indole and phenol. The helix to coil transition and the denaturation-produced solvent perturbation of the amide group must contribute less than 10% ...
Thus, barrier crossing between extended and compact forms of CaM which is normally a rare event due to the repulsive electrostatic interactions between the two lobes is facilitated by protonation of high pKa residues. The results delineate how pH changes might be utilized in the cell to achieve ...