By Michael Wink

Molecular biotechnology keeps to triumph, as this textbook testifies - edited via one of many educational pioneers within the box and written through skilled pros. This thoroughly revised moment variation covers the whole spectrum, from the basics of molecular and phone biology, through an summary of normal equipment and applied sciences, the appliance of a few of the "-omics", and the advance of novel drug objectives, correct as much as the importance of method biology in biotechnology. the total is rounded off by means of an advent to commercial biotechnology in addition to chapters on corporation origin, patent legislations and advertising and marketing.
the hot variation features:
- huge structure and whole colour throughout
- confirmed constitution in response to fundamentals, equipment, major subject matters and monetary perspectives
- New sections on method biology, RNA interference, microscopic recommendations, excessive throughput sequencing, laser purposes, biocatalysis, present biomedical purposes and drug approval
- Optimized educating with studying pursuits, a word list containing round 800 entries, over 500 vital abbreviations and additional reading.
the single source when you are heavily attracted to the topic.

Bonus fabric on hand on-line at no cost: www.wiley-vch.de/home/molecbiotech

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Extra resources for An Introduction to Molecular Biotechnology- Fundamentals, Methods and Applications

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Experiments in structural biology have already shown that the binding of a ligand in a binding site functions according to the lock-and key principle. The binding site has a specific spatial structure in which a ligand fits selectively. Binding of the ligand involves the formation of several noncovalent bonds (Fig. 15) between the functional groups of the ligand and those of the protein. Binding generally brings about a change of the protein conformation (induced fit). The binding site is not formed by amino acid residues that lie beside each other on the peptide chain, but often consists of amino acids located in different parts of a peptide chain and spatially form a binding site by appropriate specific folding (Fig.

Hydrophobic attractions. 8 summarizes the most common hydrogen bonds present in a cell. Electronegative atoms, such as oxygen and nitrogen, try to withdraw electrons from neighboring atoms such as hydrogen. This results in oxygen and nitrogen having a slight negative charge, while hydrogen is slightly positively charged. Positive and negative charges attract one another. The resulting attractions are known either as hydrogen bonds or hydrogen bridges. 3 Structure and Function of Proteins 17 Fig.

18). During the bio- 24 2 Structure and Function of Cellular Macromolecules Fig. 19 Structure of the DNA double helix. The spatial orientation of the base pairs in the double helix and the principle of complementary base pairing between A and T and G and C, respectively, via the formation of hydrogen bonds. (A) Schematic structure of the double helix. (B) Structural formulae. synthesis of the nucleic acids, the respective nucleotide triphosphates are needed whose phosphoric acid anhydride bonds are especially rich in energy.

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An Introduction to Molecular Biotechnology- Fundamentals, Methods and Applications by Michael Wink


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