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Since chemical changes such as those arising from mutations can alter the dynamical states and these alterations, if significant, must be distinctly sensed by the residues in different regions of the protein [32],[33], we next analyzed the differential effects of the mutations on the internal dynamics of the protein [Figure 3].
Genetic mutations can alter the virus' surface proteins.
However, point mutations can alter the RFLP patterns, making the interpretation of the results difficult.
Mutations can alter protein conformations in the same way that allosteric small molecules do.
This also provides deeper insights into how single-site mutations can alter the selectivity profile of closely related ligands against a target protein.
These differential effects provide the first evidence that p97 cofactors and disease mutations can alter p97 inhibitor potency and suggest the possibility of developing context-dependent inhibitors of p97.
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Still these simulations are sufficient to reveal how a single mutation can alter the reaction pathway.
IDH mutation can alter protein expression through epigenetic modifications, redox homeostasis and metabolism of glucose, glutamine (Gln) and fatty acids.
Moreover, while it is interesting to comprehend how a polymerase accomplishes this feat to achieve a certain fidelity in DNA replication, it is equally interesting to investigate how a single residue mutation can alter its fidelity.
Usually, a single mutation is not enough to result in malignant growth, but there are plenty of different combinations of mutations which can alter the expression biochemical pathways leading to the same phenotypic effect [ 3].
Mutations, which can alter amino acid constitution, contribute greatly to protein evolution.
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