When hemoglobin is oxygenated is it to as the T state. Most polar residues face

Question

When hemoglobin is oxygenated is it to as the T state. Most polar residues face the outside of the protein and interact with solvent. Thick filaments are composed almost entirely of a single type of protein actin, Sterically allowed conformations have Phi and Psi values that would bring atoms closer than the corresponding van der Waals distance A rigid, planar structure between at least two amino acids consisting of about 40% double bond character is characteristic of a hydrogen bond. With regard to torsion angles in a polypeptide backbone psi (phi) angles are located between the a carbon and N bond and the phi (psi) angles are located between the a carbon and C bond. Calcium concentration triggers the conformational change in the troponin-tropomyosin complex that exposes the site on actin where the myosin head binds Alpha helices have an electrostatic dipole moment, but beta sheets do not.

Explanation / Answer

ans1-False

When hemoglobin is bound to O2, it is called oxyhemoglobin. This is the relaxed (R ) state.

ans2-True

Most polar residues face the outside of protein and interact with solvent but may be buried if H-bonding and charge is satisfied

ans-3 False

Thick filaments are composed of contractike protein myosin only.

The proteins in thin filaments are actin as well as two another protein tropomyosin, and troponin.

ans4-False

Torsion angles phi abd shi values provides the flexibility required for the polypeptide backbone to accept a certain fold.

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