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Principles and Practice of Bioanalysis1
Log In Sign Up. Download Free PDF. Download PDF. A short summary of this paper. This book, or parts thereof, may not be reproduced in any form or by any means, electronic or mechanical, including photocopying, recording or any information storage and retrieval system now known or to be invented, without written permission from the Publisher. For photocopying of material in this volume, please pay a copying fee through the Copyright Clearance Center, Inc.
In this case permission to photocopy is not required from the publisher. At exactly this time, it seems imperative to provide a small introductory textbook covering the most frequently used instru- mental methods of analytical chemistry in molecular biology.
The increasingly interdisciplinary nature of modern research makes it essential for researchers of different backgrounds to have at least a minimal understanding of neighbouring sciences if they are to communicate effectively. Of course, each individual subunit could be found in yet another biochemistry, mass spectrometry, separations or analytical chemistry text- book.
In the light of these facts, it seems appro- priate for us to write a new book concerning the various aspects of biomolecular analysis. This book is aimed primarily at chemistry students, but is also intended to be a useful reference for students, lecturers and industrial researchers in biological and medicinal sciences who are interested in bioanalysis techniques.
It is assumed that the basic principles and instrumental techniques of analytical chemistry are already common knowledge. The priorities that govern the choice of instrumental techniques for the analysis of molecules such as DNA and proteins are radically different to those applicable to classical analytical chemistry see Summary of Chapter 1.
Whereas samples containing small molecules can be characterised by gas or liquid chromatography, when it comes to DNA sequencing or proteomic analysis, there is a sudden need for sheer separation power. Hence, students must have as clear an understanding of isoelectric focussing or 2D slab gel separation as they would of conventional chromatography. Other methods described in this book may be completely new to the chemist.
This is followed by several chapters describing various instrumental techniques and bioanalytical methods. Instead of being a comprehensive reference or textbook, it is intended that this book should provide introductory reading, perhaps alongside a taught course.
A list of references is given at the end of each chapter, should further information be required on any particular subject. Hopefully, this book will be well received by both teachers and students, par- ticularly in a time when techniques of bioanalysis should be familiar to every chemistry graduate. The authors would like to thank Dr. Alexander Iles for his comments on the manuscript. Chemists are likely to be familiar with certain biomolecules such as carbo- hydrates and lipids from their organic chemistry lectures.
However, many do not have a clear understanding of the composition and function of other biomolecules such as proteins and DNA. This chapter introduces the biomolecules, which are the target of the analytical methods described in the following chapters. They can connect to each other via peptide bonds to form long chains.
Proteins may consist of thousands of amino acids and can have molecular weights of up to several million Dalton Da. Shorter chains of up to a few hundred amino acids are referred to as peptides. The sequence of the amino acids within the molecule is essential for the structure and function of proteins and peptides in biological processes. It consists of a tetrahe- dral carbon atom C-alpha connected to four groups: a basic amino group —NH2 , an acidic carboxyl group —COOH , a hydrogen atom —H and a substituent group —R , which varies from one amino acid to another.
Amino acids are chiral with the exception of glycine, where the R substituent is a hydrogen atom. In addition, there are aliphatic, aromatic, hydroxyl containing and sulfur containing amino acids according to the nature of the substituent, as well as a secondary amino acid. For convenience, the names for amino acids are often abbreviated to either a three symbol or a one symbol short form. Basic amino acids. Acidic amino acids. Aliphatic amino acids. Aromatic amino acids.
Sulfur containing amino acids. Amino acids with an alcoholic hydroxyl group. Secondary amino acid. The abbreviations for the 20 natural amino acids are listed in Table 1. These naturally occurring amino acids are the building blocks of peptides and proteins. This is often referred to as the physiological pH. Natural amino acids. Doolittle, Database of nonredundant proteins, in G.
Fasman Ed. Dawson, D. Elliott, W. Elliott, K. Polar amino acids have no net charge but carry a polar group in the substituent R.
Positively charged amino acids at physiological pH are Lysine, Histidine and Arginine; whereas negatively charged amino acids are Aspartic acid and Glutamic acid. In addition to the 20 natural amino acids, there are other amino acids, which occur in biologically active peptides and as constituents of proteins. These will not be covered in this textbook. The carboxyl group of an amino acid has a pK between 1.
Hence, at physiological pH amino acids are zwitterionic. At low pH values, the carboxyl group is protonated to —COOH and the amino acid becomes positively charged. At high pH values, the amino group is deprotonated to —NH2 and the amino acid becomes negatively charged Fig. Functional groups in the substituents may have different pK values as well see Table 1. This is called the isoelectric point, pI.
This calculation is straightforward for mono-amino and mono-carboxylic acids, where pKi and pKj are the pK values of the amino group and the carboxylic group, respectively.
For amino acids with ionisable side chains, the calculation of the pI value is more complex. The pI values for the natural amino acids are listed in Table 1. This technique is called isoelectric focussing and will be discussed in detail in sections 3. Charge of an amino acid at different pH values: zwitterionic character at pH 7, positive charge at low pH and negative charge at high pH. Table 1. The function and structure of proteins are outlined in the following sections.
Globular proteins have a compact, spherical structure with very characteristic grooves and peaks on their surface. They are biochemical catalysts, which lower the activation energy and, thus, accelerate immensely the reaction rate of biological reactions.
An enzyme can only react with a substrate if the location of its functional groups and hydrogen bonds as well as its shape matches the active site of the enzyme. They can recognise intruders, antigens, and bind to them in a key-lock mechanism.
Enzymes and antibodies are used as molecular recognition elements in bioassays section 5. In the body, proteins also function as transport and storage media. For example, haemoglobin is responsible for the transport of oxygen in the blood stream, trans- ferrin for the transport of iron.
Ferritin is an example of a protein with a storage function, which can be found in the liver. It forms a complex with iron, and thus binds and stores the metal. In the form of hormones, polypeptides can also act as chemical messengers.
By interacting with a matching receptor, usually found in the cell membrane, they regulate a wide variety of tasks in metabolism. Other hormones control digestion, growth and cell differentiation. Hormones form a large class of chemical substances. Most hormones are polypeptides, however, some are amino acid derivates or steroids.
Fibrous proteins have a high tensile strength and mechanical stability. Their function is to provide structural support to tissues. Collagen, for example, gives connective strength to skin, bones, teeth and tendons.
Ceratin is the major component of hair and nails. This structure is crit- ical for its activity and function. Parts of the amino acid chain can be organised into helices or sheets. To describe the complex structure of proteins, four levels of organisation are distinguished: primary, secondary, tertiary and quaternary structures.
Primary structure The sequence of amino acids determines the primary structure of a protein. The amino acids are connected to each other in a head-to-tail fashion by formation of a peptide bond Fig.
Two amino acids connected via a peptide bond are called a dipeptide, three acids a tripeptide and so on. With an increasing number of acids in the sequence, the molecules are referred to as oligopeptides and polypeptides. Peptide bond formation from two amino acids. Double bond character of the C—N bond in a peptide.
Hence, the peptide unit NH—CO is rigid.
Principles and Practice of Bioanalysis
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Principles and Practice of Bioanalysis provides a guide to the methods available and the techniques currently used in this field. It provides up to the minute information and guidance on the methods and strategy used in developing and running ultra-trace analyses for drugs, metabolites and other substances. Pris: kr. Skickas inom vardagar.
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