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A network of alternative conformations in catalase (Protein Data Bank code: 1gwe) with diverse properties. Multiple phenomena define the network: van der Waals interactions (blue dots and line segments) between sidechains, a hydrogen bond (dotted green line) through a partial-occupancy water (brown), coupling through the locally mobile backbone (black), and perhaps electrostatic forces between ...
where is the stability of the protein in water and [D] is the denaturant concentration. Thus the analysis of denaturation data with this model requires 7 parameters: Δ G w {\displaystyle \Delta G_{w}} , Δ n {\displaystyle \Delta n} , k , and the slopes and intercepts of the folded and unfolded state baselines.
Protein folding must be thermodynamically favorable within a cell in order for it to be a spontaneous reaction. Since it is known that protein folding is a spontaneous reaction, then it must assume a negative Gibbs free energy value. Gibbs free energy in protein folding is directly related to enthalpy and entropy. [12]
This value corresponds to the amount of free energy contributed to the stability of the protein by the salt bridge. Figure 5. Titration curve between the wild-type (blue) and the mutant (red) The second method utilizes nuclear magnetic resonance spectroscopy to calculate the free energy of the salt bridge. A titration is performed, while ...
When a protein folds, the titratable amino acids in the protein are transferred from a solution-like environment to an environment determined by the 3-dimensional structure of the protein. For example, in an unfolded protein, an aspartic acid typically is in an environment which exposes the titratable side chain to water.
The main factors affecting membrane fluidity are environmental (ie. temperature), and compositionally. [3] One way to increase membrane fluidity is to heat up the membrane. Lipids acquire thermal energy when they are heated up; energetic lipids move around more, arranging and rearranging randomly, making the membrane more fluid.
Protein degradation occurs in proteostasis when the cellular signals indicate the need to decrease overall cellular protein levels. The effects of protein degradation can be local, with the cell only experiencing effects from the loss of the degraded protein itself or widespread, with the entire protein landscape changing due to loss of other ...
This work provides site-centred radial charge densities of the ions' interacting atoms (to approximate the electrostatic potential energy of interaction), and these appear to quantitatively correlate with many reported Hofmeister series for electrolyte properties, reaction rates and macromolecular stability (such as polymer solubility, and ...