Explain, what role can a minor conformer (1% of the total protein conformational

Question

Explain, what role can a minor conformer (1% of the total protein conformational species) play for the activity of an enzyme? In other words, if 99% of the protein molecule belongs to the "native fold", why and how could the remaining 1% be relevant for its function? For three spectroscopic methods- Fluorescence, UV spectroscopy, Solution NMR spectroscopy-explain if the technique can or cannot be used to probe the minor (1%) conformational species and why. Fluorescence UV spectroscopy Solution NMR spectroscopy

Explanation / Answer

roteins are dynamic molecules that must move to function. For proteins that are catalytic (i.e., enzymes) some of these motions regulate their catalytic function. Although plausible models of the allosteric regulation of enzymatic reactions by protein conformation were first proposed 40 years ago to great acclaim, the elucidation of the physical basis for this control has taken a steady, decades-long course and is still incomplete. Much has been learned in the intervening decades about the physical basis of allostery, for instance the relationship between conformational heterogeneity and ligand binding, and the stereochemical basis of allostery in a prototypical protein. However, answers to a number of questions, such as the quantitative dependence of an enzymatic reaction barrier on structurally characterized protein conformations, have been elusive.

The minor conformer can be detected using solution NMR spectroscopy. The enantiotopic or diastereotopic hydrogens as well as carbons give different peaks in NMR spectrum From the relative integration ratio of the peaks due to different conformers the population of the conformers can be calculated.

Related Questions

Navigate

• Browse (All)
• Browse E
• Subjects

---

---

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.