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Protein bonds energy

Using bond energies, estimate AH for protein formation, per mole of amino add added to the chain. Does this value seem reasonable ... [Pg.633]

Dynein, kinesin, and myosin are motor proteins with ATPase activity that convert the chemical bond energy released by ATP hydrolysis into mechanical work. Each motor molecule reacts cyclically with a polymerized cytoskeletal filament in this chemomechanical transduction process. The motor protein first binds to the filament and then undergoes a conformational change that produces an increment of movement, known as the power stroke. The motor protein then releases its hold on the filament before reattaching at a new site to begin another cycle. Events in the mechanical cycle are believed to depend on intermediate steps in the ATPase cycle. Cytoplasmic dynein and kinesin walk (albeit in opposite... [Pg.16]

The ONIOM protein system contains the substrate, methylmalonyl-CoA, bound to the active site, the cofactor (AdoCbl) and all amino acids within a 15-A radius from the cobalt atom. The active-site selection contains a truncated AdoCbl and the imidazole ring of its lower ligand. The QM part was calculated using the BP86 functional [31, 72] because it gives better agreement with experimental Co—C bond energies [73, 74], This a different choice of functional compared to the other studies in the present review. [Pg.44]

Fournier and DePristo96 calculated bond energies in several small compounds containing disulfide bonds which are known to stabilize the tertiary structure of proteins. Bond dissociation energies are generally overestimated when LDA(SVWN) is used whereas the PW86/P86 functional brings them to within 5 kcal/mol of experimental values. [Pg.97]

Tab. 3.4 Shift of the C-O and Fe-C stretch frequencies relative to the isolated heme-CO system for each of the protein conformations l-V. Hydrogen bond energies are also listed. Distances are given in A, frequencies in cm-1 and energies in kcal mol-1. Tab. 3.4 Shift of the C-O and Fe-C stretch frequencies relative to the isolated heme-CO system for each of the protein conformations l-V. Hydrogen bond energies are also listed. Distances are given in A, frequencies in cm-1 and energies in kcal mol-1.
Toxicant-protein complexes that utilize relatively weak bonds (energies of the order of hydrogen bonds or less) readily associate and dissociate at physiological temperatures, and the law of mass action applies to the thermodynamic equilibrium ... [Pg.101]

Table 3-4 Bond Energies of the Bonds Involved in Protein Structure... Table 3-4 Bond Energies of the Bonds Involved in Protein Structure...

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See also in sourсe #XX -- [ Pg.117 ]




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