By David Hames, Nigel Hooper
BIOS immediate Notes in Biochemistry, Fourth variation, is the appropriate textual content for undergraduates searching for a concise creation to the topic, or a research consultant to exploit ahead of examinations. every one subject starts with a precis of crucial facts-an perfect revision checklist-followed via an outline of the topic that specializes in middle info, with transparent, uncomplicated diagrams which are effortless for college kids to appreciate and remember in essays and assessments.
BIOS quick Notes in Biochemistry, Fourth variation, is absolutely up to date and covers:
- Amino acids and proteins
- Studying proteins
- Membranes and telephone signalling
- DNA constitution and replication
- RNA synthesis and processing
- Protein synthesis
- Recombinant DNA technology
- Carbohydrate metabolism
- Lipid metabolism
- Respiration and energy
- Nitrogen metabolism
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Additional resources for Biochemistry (Instant notes)
The different types of collagen are found in different locations in the body. Biosynthesis: overview The collagen polypeptides are post-translationally modified by hydroxylation and glycosylation on transport through the rough endoplasmic reticulum and Golgi. The three polypeptides form the triple-helical procollagen which is secreted out of the cell. The extension peptides are removed to form tropocollagen which then aggregates into a microfibril and is covalently crosslinked to form the mature collagen fiber.
Also included under primary structure is the location of any other covalent bonds. These are primarily disulfide bonds between cysteine residues that are adjacent in space but not in the linear amino acid sequence. These covalent cross-links between separate polypeptide chains or between different parts of the same chain are formed by the oxidation of the SH groups on cysteine residues that are juxtaposed in space (Fig. 4). The resulting disulfide is called a cystine residue. Disulfide bonds are often present in extracellular proteins, but are rarely found in intracellular proteins.
The basic amino acids arginine (Arg, R) and lysine (Lys, K) have positively charged side-chains, whilst the side-chain of histidine (His, H) can be either positively charged or uncharged at neutral pH. The side-chains of the acidic amino acids aspartic acid (Asp, D) and glutamic acid (Glu, E) are negatively charged at neutral pH. The amide side-chains of asparagine (Asn, N) and glutamine (Gln, Q), and the hydroxyl side-chains of serine (Ser, S) and threonine (Thr, T) are uncharged and polar, and can form hydrogen bonds.