Guide to Biochemistry by James C. Blackstock (Auth.)

By James C. Blackstock (Auth.)

This illustrated reference guide offers scholars of the organic sciences with crucial easy details, to inspire the knowledge of options and supply a grounding within the middle of biochemical wisdom. Amino acids, molecules, proteins, enzymes and lipids are mentioned intimately

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This is why maltose contains an a - ( 1 ^ 4 ) bond [and not an a - ( 4 - > l ) bond]. In trehalose, the anomeric carbon atoms o f both units are involved in the linkage. Since trehalose contains the same monomeric units, there is no problem. However, in sucrose the anomeric carbon atoms o f different monomeric units are involved in the linkage. 7 Structures of some glucose-containing disaccharides. (a) Homodisaccharides. (b) Heterodisaccharides CH2OH OH (D-Galactose) '^""^ Lactose OH (o-Glucose) OH Isomaltose CH2OH CH2OH , (D-Glucose) OH OH ß-(1-4) bond CH2OH Cellobiose CH2OH CHoOH (D-Fructose) Sucrose OH OH "bond" end (a) 0" Non-reducing Non-reducing Trehalose ü-(1-^2)bond or ß-(2-^l)bond end (b) Polysaccharides: homoglycans the glycosidic bond o f sucrose is α-(1->2) when considered from glucose but β-(2->1) when con­ sidered from fructose.

The distances between major recurrent features is termed major periodicity and between minor recurrent features is the minor periodicity. X-ray crystallography creates the impression that each atom in the protein molecule is firmly fixed in position. This view of a static structure is being replaced by an appreciation of the dynamic nature of the molecule in which the atoms of the protein are in a state of constant motion. Therefore, X-ray diffraction studies produce an average position around which each atom moves.

The sixth position of the iron atom is vacant and available for the binding of oxygen. Once bound, the oxygen is stabilized by hydrogen bonding to the imidazole ring of the E7 histidine. 10. 3). The structural information gained from the analysis of myoglobin served as the basis for hypotheses on tertiary structure. However, myoglobin is an atypical globular protein since it lacks cysteinyl residues (no disulphide bonds) and ~-con­ formation, but contains a very large proportion of a-helical structure.

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