By Michael Wink
Molecular biotechnology keeps to triumph, as this textbook testifies - edited via one of many educational pioneers within the box and written by way of skilled pros. This thoroughly revised moment version covers the full spectrum, from the basics of molecular and mobilephone biology, through an outline of normal tools and applied sciences, the appliance of a number of the "-omics", and the advance of novel drug pursuits, correct as much as the importance of approach biology in biotechnology. the entire is rounded off by means of an creation to business biotechnology in addition to chapters on corporation beginning, patent legislation and advertising.
the hot version features:
- huge structure and entire colour throughout
- confirmed constitution in accordance with fundamentals, tools, major themes and fiscal perspectives
- New sections on procedure biology, RNA interference, microscopic innovations, excessive throughput sequencing, laser purposes, biocatalysis, present biomedical functions and drug approval
- Optimized instructing with studying pursuits, a thesaurus containing round 800 entries, over 500 vital abbreviations and additional reading.
the one source when you are heavily drawn to the topic.
Bonus fabric on hand on-line for free: www.wiley-vch.de/home/molecbiotech
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Additional info for An Introduction to Molecular Biotechnology- Fundamentals, Methods and Applications
B) Schematic representation of the secondary structure of 16S rRNA. , 2002, p. ) (C) An example of 23S rRNA (from Haloarcula marismortui, a halophilic red Archaeon found in the Dead Sea) with six domains (Domain I–VI). , 2002, p. 4 Structure of Nucleotides and Nucleic Acids (DNA and RNA) 27 Fig. 21 Structure and function of a hammerhead ribozyme. RNA interference (RNAi) describes a widely distributed phenomenon in which double-stranded RNA molecules lead to the breakdown of complementary mRNA.
A-Helix structures and b-pleated sheet structures arise from hydrogen bonds between the N–H and C=O groups in the backbone of the polypeptide chain. Functional groups on the side chains do not take part in these structural elements. 11 describes the structure of helices and pleated sheets more precisely. Other structures include loops and random coils. A b-sheet structure element is often found at the inner core of many proteins. The b-pleated sheet can appear between neighboring polypeptide chains that have the same orientation (parallel chain).
In comparison to covalent bonds (bond strength of 348–469 kJ mol–1), noncovalent bonds are 5–100 times weaker. Many noncovalent bonds that are present simultaneously can work cooperatively, leading to the formation of stable and thermodynamically favored structure elements in polypeptides. Hydrophobic amino acid residues cluster together, in order to lock water out. In polypeptides this can lead to a globular tertiary structure, while the hydrophobic residues are oriented towards the inside, and the polar and charged residues are oriented towards the outside (Fig.
An Introduction to Molecular Biotechnology- Fundamentals, Methods and Applications by Michael Wink