Biochemistry (Instant notes) by David Hames, Nigel Hooper

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:

  • Cells
  • Amino acids and proteins
  • Studying proteins
  • Enzymes
  • 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

Show description

Read Online or Download Biochemistry (Instant notes) PDF

Best molecular biology books

Handbook of Soil Sciences

An evolving, dwelling organic/inorganic overlaying, soil is in dynamic equilibrium with the ambience above, the biosphere inside of, and the geology lower than. It acts as an anchor for roots, a purveyor of water and nutrition, a place of abode for an unlimited neighborhood of microorganisms and animals, a sanitizer of our surroundings, and a resource of uncooked fabrics for building and production.

Genes, Information, and Semiosis

As much as the center of the twentieth century, biologists studied genes with no seeing them as informational buildings; info conception was once an engineering software now not facing the which means of messages; and, semiotics, the learn of indicators and their that means, dealt purely with human tradition. this present day - after growth in molecular biology and a naturalist flip as a rule semiotics - researchers are starting to detect that genes, info and semiosis, or signal motion, can not be understood in isolation.

Protein Design: Methods and Applications

Protein layout: strategy and functions, moment version expands upon the former variation with present, particular rules on how you can process a possible protein layout venture. With new chapters on metals as structure-forming components and useful websites, the layout and characterization of fluorinated proteins, top-down symmetric deconstruction and the layout of protein libraries and novel or repurposed enzymes.

Understanding PCR. A Practical Bench-Top Guide

Figuring out PCR: a realistic Bench-Top advisor can provide all the details you must plan your first PCR, from reagents to stipulations to research and past. it's a consumer pleasant e-book that has step by step easy protocols, which might be tailored in your wishes. contains worthwhile info similar to the place to reserve your reagents and simple troubleshooting tricks and information.

Additional resources for Biochemistry (Instant notes)

Example text

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.

Download PDF sample

Rated 4.49 of 5 – based on 25 votes