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Showing 1 to 5 of 5 for “"protein kinetics"”.
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Investigation of protein-protein interaction using atomic force microscopy
<p>Single-molecule approaches to measuring the kinetics of protein dissociation have the advantage that measurements can be performed in native environments, such as living cells, where concentrations of target molecules may be quite low. In addition, single molecule approaches allow for the …
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Pressure and temperature dependence of myoglobin kinetics
Recombination kinetics of carbon monoxide to myoglobin and protoheme are measured from 0.1 MPa to 190 MPa (1 bar to 1.9 kbar) at temperatures from 290K to 60K using flash photolysis. The role of the protein structure is elucidated by comparison of myoglobin kinetics with those of protoheme whose …
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Long lived states induced by extended illumination of carbonmonoxy-myoglobin
"Myoglobin is a heme-protein that binds small ligands, such as 02 and CO. A photon of visible light absorbed by the protein can break the protein ligand bond. At low temperatures (> 160K) the kinetics of recombination of photodissociated carbonmonoxymyoglobin are non-exponential, having amplitude …
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Interactions between nucleoid associated proteins and DNA in the presence of mechanical and chemical forces
… smaller cell, but must also be accessible to proteins responsible for biological processes. Architectural proteins assist with this large-scale arrangement of DNA to achieve the correct balance between these two competing requirements. The structural proteins that interact with DNA in …
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Markov state modeling of binding and conformational changes of proteins
Proteins are molecules that are essential for life and carry out an enormous number of functions in organisms. To this end, they change their conformation and bind to other molecules. However, the interplay between conformational change and binding is not fully understood. In this work, this …