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  1. (a) Structural features, equilibrium distribution and kinetics of six unbound (apo) protein conformations. Transitions between them occur at timescales on order of tens of microseconds. The three...

  2. The average pairwise RMSD across the holo forms of single- and multiple-domain pro-teins was found to be 0.49 and 0.52 A ̊ , respectively. The dif-ferences between the global structures of apo and holo pro-teins are more prominent than those observed across various ligand-bound conformations.

  3. 11 sie 2015 · The chain A of apo, holo and ligand-bound forms of aldehyde dehydrogenase enzyme from Streptococcus mutans was superimposed with each other to depict the changes in structural conformation in the presence of cofactor and ligand (Fig. 2). Chain A of all these three forms contains 475 amino acids.

  4. 19 maj 2021 · In this manuscript we explore the structure and stability of both apo- and holo-forms of a Rubredoxin from Marinobacter hydrocarbonoclasticus using Synchrotron Radiation Circular Dichroism (SRCD) in combination with other biochemical and spectroscopic techniques.

  5. Deuterium differences between heme-bound and apo forms were calculated using the equation D heme − D apo for each comparison and then colored according to the scale shown. A guide to the regions of each protein is shown at the far right (colored as in Fig. 1 ).

  6. 18 lut 2021 · Understanding both how natural and synthetic ligands bind to GPCRs and how agonists activate receptors to recruit transducer proteins is critical to understanding how the body regulates the flow of complex information that is presented to different cells and tissues to enable coordinated biological responses.

  7. 1 sie 2015 · Low molecular weight protein tyrosine phosphatases (LMW-PTP, EC 3.1.3.48) are a family of single-domain enzymes with molecular weight up to 18 kDa, expressed in different tissues and considered attractive pharmacological targets for cancer chemotherapy.

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