Book contents
- Frontmatter
- Contents
- Preface to the seventh edition
- List of contributors
- List of abbreviations
- 1 Basic principles
- 2 Cell culture techniques
- 3 Centrifugation
- 4 Microscopy
- 5 Molecular biology, bioinformatics and basic techniques
- 6 Recombinant DNA and genetic analysis
- 7 Immunochemical techniques
- 8 Protein structure, purification, characterisation and function analysis
- 9 Mass spectrometric techniques
- 10 Electrophoretic techniques
- 11 Chromatographic techniques
- 12 Spectroscopic techniques: I Spectrophotometric techniques
- 13 Spectroscopic techniques: II Structure and interactions
- 14 Radioisotope techniques
- 15 Enzymes
- 16 Principles of clinical biochemistry
- 17 Cell membrane receptors and cell signalling
- 18 Drug discovery and development
- Index
- Plate section
- References
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8 - Protein structure, purification, characterisation and function analysis
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Book contents
- Frontmatter
- Contents
- Preface to the seventh edition
- List of contributors
- List of abbreviations
- 1 Basic principles
- 2 Cell culture techniques
- 3 Centrifugation
- 4 Microscopy
- 5 Molecular biology, bioinformatics and basic techniques
- 6 Recombinant DNA and genetic analysis
- 7 Immunochemical techniques
- 8 Protein structure, purification, characterisation and function analysis
- 9 Mass spectrometric techniques
- 10 Electrophoretic techniques
- 11 Chromatographic techniques
- 12 Spectroscopic techniques: I Spectrophotometric techniques
- 13 Spectroscopic techniques: II Structure and interactions
- 14 Radioisotope techniques
- 15 Enzymes
- 16 Principles of clinical biochemistry
- 17 Cell membrane receptors and cell signalling
- 18 Drug discovery and development
- Index
- Plate section
- References
Summary
IONIC PROPERTIES OF AMINO ACIDS AND PROTEINS
Twenty amino acids varying in size, shape, charge and chemical reactivity are found in proteins and each has at least one codon in the genetic code (Section 5.3.5). Nineteen of the amino acids are α-amino acids (i.e. the amino and carboxyl groups are attached to the carbon atom that is adjacent to the carboxyl group) with the general formula RCH(NH2)COOH, where R is an aliphatic, aromatic or heterocyclic group. The only exception to this general formula is proline, which is an imino acid in which the -NH2 group is incorporated into a five-membered ring. With the exception of the simplest amino acid glycine (R = H), all the amino acids found in proteins contain one asymmetric carbon atom and hence are optically active and have been found to have the l configuration.
For convenience, each amino acid found in proteins is designated by either a three-letter abbreviation, generally based on the first three letters of their name, or a one-letter symbol, some of which are the first letter of the name. Details are given in Table 8.1.
Since they possess both an amino group and a carboxyl group, amino acids are ionised at all pH values, i.e. a neutral species represented by the general formula does not exist in solution irrespective of the pH.
Information
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- Information
- Principles and Techniques of Biochemistry and Molecular Biology , pp. 300 - 351Publisher: Cambridge University PressPrint publication year: 2010
References
(2004). Protein Purification Protocols. Totowa, NJ: Humana Press. (Detailed theory and practical procedures for a range of protein purification techniques.)Google Scholar
(2005). Proteomics Protocols Handbook. Totowa, NJ: Humana Press. (Theory and techniques of a spectrum of methods applied to proteomics.)CrossRefGoogle Scholar
(2006). New and Emerging Proteomics Techniques. New York: Humana Press. (In-depth details of a range of proteomics techniques.)Google Scholar
(2008). Functional Proteomics. New York: Humana Press. (Comprehensive coverage of functional proteomics including protein analysis and mass spectrometry.)CrossRefGoogle ScholarPubMed
, and (2008). Basic Methods in Protein Purification and Analysis: A Laboratory Manual. New York: CSH Press. (A comprehensive collection of protein purification methods.)Google Scholar
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