By Thomas E. Creighton
DNA, RNA and proteins are surely crucial organic molecules. Being huge macromolecules, their actual, chemical and organic houses can vary dramatically from these of the monomers from which they're made. defined listed below are their fundamental, secondary, tertiary and quaternary constructions; their evolutionary origins; their unfolding and refolding; their chemical synthesis and manipulation; their actual interactions with different molecules, which regularly bring about catalysis of chemical reactions in a single or either one of them; and a number of the ways that the catalytic actions of enzymes are managed and controlled. colour is used liberally in the course of the quantity to reinforce the various illustrations. it is a accomplished reference for chemists, biologists and scholars.
desk of Contents
Section 1. Macromolecules 1. Configurations and Conformations
Section 2. Nucleic Acids 2. DNA constitution
three. DNA Topology
four. RNA constitution
five. Denaturation, Renaturation and Hybridization of Nucleic Acids
6. Manipulating Nucleic Acids
Section three. Proteins 7. Polypeptide constitution
eight. Polypeptide Conformation
nine. Protein constitution
10. actual houses of Folded Proteins
eleven. Protein Denaturation: Unfolding and Refolding
Section four. features 12. Ligand Binding via Proteins
thirteen. Nucleic Acid-Protein Interactions
15. Enzyme rules
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Extra info for Biophysical Chemistry of Nucleic Acids and Proteins
It can be specified by the helical repeat, the number of monomers per turn (which need not be an integer), and the pitch of the helix, the vertical distance between adjacent turns. Whether the helix is left- or right-handed is determined by the sense of the rotation needed to advance along z: the helix should be considered a screw that needs to be advanced by turning it with a screwdriver. If the direction of rotation is that indicated by the fingers of the right hand, the helix is right-handed.
1998) J. Mol. Biol. 280, 421–430. DNA structure CHAPTER 2 37 The heat capacities of the bases are significantly more positive than would be predicted on the basis of just their surface areas accessible to water. N, O and P atoms of small molecules and amino acids make negative contributions to Cp, probably because they increase the distortion of water hydrogen bonds. The anomalous properties of the nucleobases may indicate that many of their polar atoms are hydrated by water molecules whose hydrogen bonds are less distorted than in bulk water, which would produce a more positive Cp.
USA 101, 12491–12496. Secondary structures in long compact polymers. R. Oberdorf et al. (2006) Phys. Rev. E 74, 051801. 1. End-to-end Distances Of greatest interest with random polymers are the averages and the variation of their physical dimensions. 23) where n is the number of linkages between monomers (= N – 1, where N is the number of monomers in the chain) and l is the distance between monomers in the polymer backbone. 23 indicate that it is the average over all conformations, and the subscript zero refers to the unperturbed state.
Biophysical Chemistry of Nucleic Acids and Proteins by Thomas E. Creighton