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By Phoebe A. Rice, Carl C. Correll

This e-book presents either in-depth history and updated info during this sector. The chapters are equipped via basic issues and rules, written via specialists who illustrate themes with present findings. themes lined contain: - the function of ions and hydration in protein-nucleic acid interactions- transcription elements and combinatorial specificity- oblique readout of DNA series- single-stranded nucleic acid binding proteins- nucleic acid junctions and proteins, - RNA protein attractiveness- attractiveness of DNA harm. will probably be a key reference for either complex scholars and validated scientists wishing to expand their horizons.

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Example text

Alternatively, ribonucleases (Chapter 7) can use this strategy to move the RNA from an inactive form to an active form, in which the nucleophilic 2 0 -hydroxyl group is positioned in-line with the scissile phosphate bond, and thereby poised for attack. RNAs, like proteins, can misfold, and are perhaps even more susceptible to such problems. RNA chaperones have evolved to alleviate this problem. These proteins can accelerate RNA annealing, strand displacement and/or helix destabilizing activities to guide the RNA into a functional form (Chapter 9).

Free protein models were as follows: apo-EcoRI,167 missing residues modeled according to Creamer and Rose;43,44 BamHI, ASA of residues 79–91 of undocked protein from nonspecific complex (1ESG) substituted for same region on undocked protein from specific complex; apo-EcoRV (1RVE). The net change in ASA on complex formation was calculated as DASA ¼ ASAcomplex–(ASAprotein + ASADNA). 3. b The free energy contribution of the hydrophobic effect DG1HE was calculated as described in the text. c Changes upon binding in the number of macromolecule-associated waters (DNw) from DASA computation use surface occupancy of 101A˚2 per H2O and are corrected for retained interfacial H2O: EcoRI and BamHI (50 waters); EcoRV (56 waters).

RNAs, like proteins, can misfold, and are perhaps even more susceptible to such problems. RNA chaperones have evolved to alleviate this problem. These proteins can accelerate RNA annealing, strand displacement and/or helix destabilizing activities to guide the RNA into a functional form (Chapter 9). DNA and RNA helicases also rearrange nucleic acid structure, but unlike chaperones they hydrolyze ATP to drive duplex unwinding and/or to dislodge bound proteins (refs. 10–12 are excellent recent reviews).

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