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Overall, this seems to be a small difference, but locally two extra charges can affect the interaction between two proteins.
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This charging can affect numerous defect properties such as structure, thermal diffusion rates, trapping and recombination rates for electrons and holes, and luminescence quenching rates.
We hypothesized that altering the physical properties of multi-walled CNTs (MWNTs -antigen conjugates, e.g. length and surface charge, can affect the internalization of MWNTs -antigeny Dconjugatesthe.gnduced immune response potency.
Because a large amount of electrons are excited and emitted from the sample, the sample is always positively charged and the electric field caused by the charge can affect the measured kinetic energy of photoelectron.
The electric field caused by the charge can affect the measured kinetic energy of photoelectrons, so all XPS spectra were calibrated by the C 1s peak (284.6 eV) from contamination to compensate the charge effect.
Surface charge can affect membrane protein function by a variety of mechanisms, in addition to affecting the voltage sensed by the protein.
Furthermore, factors such as peptide charge can affect the efficiency of nanocomplex unpacking, which may in turn affect the availability of siRNA inside the cytosol to bind to mRNA transcripts and participate in RNAi-mediated gene silencing.
Structure guided mutational studies showed that the N-terminal negatively charged and C-terminal positively charged residues can affect the secretion of EvpC.
The effect of implementing more sophisticated partial charge calculations would be interesting, as a recent study has suggested that the method used for partial charge calculations can affect QSAR predictive accuracy [58].
The observed surface charge accumulation can affect parameters and performance of field effect transistors on III V NWs [32]. Figure 2 Projection of charge distribution on the plane of the cross section for III V NWs with small {112} facets and largest considered diameter of about 4 nm.
ii) Isoelectric point (pI) is the pH at which a protein carries no net electrical charge, which can affect its solubility at a given pH.
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