By Hames D., Hooper N.

An enormous replace of the hugely well known moment version, with alterations within the content material and company that replicate advances within the topic. As with the 1st variations, the 3rd version of immediate Notes in Biochemistry offers the basic proof of biochemistry with special motives and transparent illustrations. it is also new and increased subject matters similar to cytoskeleton, molecular automobiles, bioimaging, biomembranes, phone signaling, protein constitution and enzymes legislation.

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The resolution of the scanning electron microscope is 10 nm, some 100fold less than that of the transmission electron microscope. Section A – Cell structure and imaging A5 C ELLULAR FRACTIONATION Key Notes Isolating cells and their parts: overview Animal and plant tissues contain a mixture of cell types, and most cells contain multiple subcellular organelles. In order to study cells and organelles in isolation, it is desirable to have a homogeneous population of cells. Flow cytometry Individual cells can be identified using a flow cytometer.

Using recombinant DNA techniques (see Topics I4 and I6), the DNA encoding GFP can be tagged on to the DNA sequences encoding other proteins, and then introduced into living cells in culture or into specific cells of a whole animal. Cells containing the introduced gene will then produce the protein tagged with GFP which will fluoresce green under the fluorescent microscope. The localization and movement of the GFP-tagged protein can then be studied in living cells in real time. g. cyan fluorescent protein (CFP) and yellow fluorescent protein (YFP), allowing several proteins to be visualized simultaneously in the same cell.

Secondary structure Secondary structure in a protein refers to the regular folding of regions of the polypeptide chain. The two most common types of secondary structure are the α-helix and the β-pleated sheet. The α-helix is a cylindrical, rod-like helical arrangement of the amino acids in the polypeptide chain which is maintained by hydrogen bonds parallel to the helix axis. In a β-pleated sheet, hydrogen bonds form between adjacent sections of polypeptides that are either running in the same direction (parallel β-pleated sheet) or in the opposite direction (antiparallel βpleated sheet).

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