This is because hydrogen-bonding groups in an unfolded protein form hydrogen bonds with water molecules. Thus the contribution of a hydrogen bond to the stability of a native protein is the small difference in hydrogen bonding free energies between the native and unfolded states (−2 to 8 kJ ∙ mol−1)

#Id: 2406

#Unit 3. Fundamental Processes

RNA polymerase performs two proofreading functions on that growing transcript

pyrophosphorolytic editing

hydrolytic editing

#Id: 2407

#Unit 3. Fundamental Processes

In the Pyrophosphorolytic editing, the enzyme uses its active site, in a simple back-reaction, to catalyze the removal of an incorrectly inserted ribonucleotide, by reincorporation of PPi.

#Id: 2408

#Unit 3. Fundamental Processes

Hydrolytic editing, is the polymerase backtracks by one or more nucleotides and cleaves the RNA product, removing the error-containing sequence.

#Id: 2409

#Unit 3. Fundamental Processes

Hydrolytic editing is stimulated by Gre factors, which both enhance hydrolytic editing function and serve as elongation stimulating factors.

#Id: 2410

#Unit 3. Fundamental Processes

The Nus proteins—joins polymerase in the elongation phase and promotes.

#Id: 2411

#Unit 3. Fundamental Processes

Both polymerase removal and repair enzyme recruitment are performed by a single protein called TRCF.