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katrin2010 [14]
3 years ago
6

Many proteins are regulated by the binding of GTP or GDP. Which form is the active state of the protein

Biology
1 answer:
Aliun [14]3 years ago
3 0

Answer:

GTP-bound form

Explanation:

Such a receptor may be associated with the GDP-regulated G-stimulant protein system. When the neurotransmitter binds to the receptor, the protein G-GDP complex is activated by separating its β subunit. When the ligand "sticks" to it, it releases GDP and allows GTP to bind. This form of the G protein that binds GTP, is the activated ("on") form of it. When it is "on" it releases signals into the cell. After a short period (seconds or less) the G protein hydrolyzes the GTP to GDP and itself "turns off".

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Answer:

(B) They may have binding sites for regulatory molecules that are separate from active sites.

(C) They generally have more than one subunit.

(E) They interconvert between a more active form and a less active form.

Explanation:

Allosteric enzymes are the regulatory enzymes that have a specific site for binding of modulator or effector molecule. The activity of these enzymes is altered by the noncovalent binding of modulators at the allosteric site. The binding of the modulator brings about a conformational change in the allosteric enzymes.

The relatively inactive conformation of these enzymes is called T state while the active conformation is the R state. Most of the allosteric enzymes have multiple subunits and deviate from Michaelis–Menten kinetics and exhibit a sigmoid saturation curve of V0 vs. [S].

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The red color of the colonies is an example of <u>a phenotype .</u>

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