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Principles and problems in physical chemistry for biochemists / Nicholas C. Price ... [et al.]

Contributor(s): Price, Nicholas C | Price, Nicholas C. Principles and problems in physical chemistry for biochemists.
Material type: materialTypeLabelBookPublisher: Oxford ; New York : Oxford University Press, 2001Edition: 3rd ed. / Nicholas C. Price ... [et al.].Description: xix, 401 p. : ill. ; 25 cm.ISBN: 0198792816 (pbk. : acidfree paper); 9780198792819.Other title: Physical chemistry for biochemists.Subject(s): Biochemistry | Chemistry, Physical and theoretical | Chemistry, Physical and theoretical -- Problems, exercises, etc | Science | Chemistry | Physical chemistry | Biology, life sciences | Biochemistry | Molecular biologyDDC classification: 541.3 PRI
Contents:
The consequences of physics and chemistry for life -- Basic thermodynamics -- Chemical potential and multiple component systems -- Binding of ligands to macromolecules -- Acids, bases and pH regulation -- Oxidation: reduction reactions and electrochemistry -- Chemical potentials and the properties of solutions -- Ideal and non-ideal solutions -- Basic chemical kinetics and single-step reactions -- Applications of chemical kinetics to multistep reactions -- Catalysis and enzyme kinetics -- Multisubstrate enzyme kinetics and enzyme inhibition -- Coupled reactions and biochemical pathways -- Quantum mechanics: particles, waves and quantisation of energy -- Electrons in atoms -- Bonding in molecules -- Interaction of molecules with electromagnetic radiation -- Non-covalent interactions and macromolecular structure.
Summary: What use is physical chemistry to the students of biology and biochemistry? This central question is answered in this book, mainly through the inclusion of worked examples and problems.
Holdings
Item type Current library Call number Copy number Status Barcode
General lending MTU Kerry North Campus Library First Floor Main 541.3 PRI (Browse shelf(Opens below)) 1 Available 38888000471031
Total holds: 0

Enhanced descriptions from Syndetics:

What use is physical chemistry to the student of biochemistry and biology? This central question is answered in this book mainly through the use of worked examples and problems. The book starts by introducing the laws of thermodynamics, and then uses these laws to derive the equations relevant to the student in dealing with chemical equilibria (including the binding of small molecules to proteins), properties of solutions, acids and bases, and oxidation-reduction processes. The student is thus shown how a knowledge of thermodynamic qualities makes it possible to predict whether, and how, a reaction will proceed.Thermodynamics, however, gives no information about how fast a reaction will happen. The study of the rates at which processes occur (kinetics) forms the second main theme of the book. This section poses and answers questions such as `how is the rate of a reaction affected by temperature, pH, ionic strength, and the nature of the reactants? These same ideas are then shown to be useful in the study of enzyme-catalysed reactions.

Rev. ed. of: Principles and problems in physical chemistry for biochemists / Nicholas C. Price and Raymond A. Dwek. 2nd ed. 1979.

Includes bibliographical references and index.

The consequences of physics and chemistry for life -- Basic thermodynamics -- Chemical potential and multiple component systems -- Binding of ligands to macromolecules -- Acids, bases and pH regulation -- Oxidation: reduction reactions and electrochemistry -- Chemical potentials and the properties of solutions -- Ideal and non-ideal solutions -- Basic chemical kinetics and single-step reactions -- Applications of chemical kinetics to multistep reactions -- Catalysis and enzyme kinetics -- Multisubstrate enzyme kinetics and enzyme inhibition -- Coupled reactions and biochemical pathways -- Quantum mechanics: particles, waves and quantisation of energy -- Electrons in atoms -- Bonding in molecules -- Interaction of molecules with electromagnetic radiation -- Non-covalent interactions and macromolecular structure.

What use is physical chemistry to the students of biology and biochemistry? This central question is answered in this book, mainly through the inclusion of worked examples and problems.

Table of contents provided by Syndetics

  • Notes to the reader (p. xv)
  • Symbols (p. xvii)
  • Introduction
  • 1. The consequences of physics and chemistry for life (p. 3)
  • The constraints imposed on a biological system by its environment
  • The constraints imposed on a biological system by physics and chemistry
  • Physical chemistry and 'Biochemists'
  • Scope of this book
  • The Energetics of Chemical Reactions
  • 2. Basic thermodynamics (p. 11)
  • What is thermodynamics?
  • Basic definitions
  • Statement of the first law of thermodynamics
  • Work and heat and internal energy
  • Work energy in chemical systems
  • The concept of enthalpy
  • Standard states
  • Enthalpy as a state function
  • The first law and direction of a reaction
  • Available energy, work and change
  • Statement of the second law of thermodynamics
  • The concept of entropy
  • Alternative expression of the second law of thermodynamics
  • The concept of free energy
  • Free energy and equilibrium
  • Thermodynamics applied to real systems
  • Molecular basis of enthalpy and entropy
  • Further reading
  • Problems
  • 3. Chemical potential and multiple component systems (p. 34)
  • The concept of chemical potential
  • Chemical potential and change
  • Spontaneous reactions and equilibria
  • Variation of chemical potential with concentration
  • Dependence of [Delta] G on concentration
  • Mass action ratios and equilibrium constants
  • Alternative view of equilibrium constants
  • Variation of equilibrium constant with temperature
  • Dependence of enthalpy and entropy on temperature
  • Measurement of the thermodynamic quantities of reactions
  • Further reading
  • Problems
  • 4. Binding of ligands to macromolecules (p. 54)
  • Ligand binding to a single site on a protein
  • Simultaneous binding of different ligands to a protein
  • A single ligand binding to multiple sites on a protein
  • The binding of multivalent ligands to multivalent proteins
  • Further reading
  • Problems
  • 5. Acids, bases and pH regulation (p. 74)
  • The ionic dissociation of water
  • The Arrhenius definition of acids and bases
  • The concept of pH
  • Conjugate acids and bases
  • Quantifying acid and base strengths
  • Relative and absolute acid and base strengths
  • Variation of pK[subscript a] with environment
  • The neutralisation of acids and bases
  • pH in biological systems
  • Buffer solutions
  • Quantifying buffer strengths
  • Regulation of pH by ion transport
  • Measurement of pH
  • Further reading
  • Problems
  • 6. Oxidation-reduction reactions and electrochemistry (p. 97)
  • Oxidation--reduction reactions
  • Electrochemical cells
  • The thermodynamics of reversible cells
  • Cells and half-cells
  • Cell and half-cell nomenclature
  • Types of half-cells
  • Electrode potentials
  • The Nernst equation
  • Potentiometric titrations
  • Concentration cells
  • Effect of temperature on cell e.m.f. values
  • Calculation of thermodynamic quantities from electrochemical data
  • The effect of non-ideality
  • Coupled oxidation--reduction processes
  • Determination of pH
  • Further reading
  • Problems
  • 7. Chemical potentials and the properties of solutions (p. 122)
  • Colligative properties
  • Osmosis
  • Osmotic pressure
  • Water potentials
  • Chemical potential of the solute
  • Determination of pH using permeable weak acids and bases
  • Equilibration of mobile solutes in the presence of charged macromolecules: the Donnan effect
  • Charged solutes and electric fields
  • Membrane potentials
  • Electrochemical gradients for ions
  • Electrochemical gradients as energy stores
  • Oxidative phosphorylation and photophosphorylation
  • Stoichiometry of proton pumping and ATP synthesis
  • Further reading
  • Problems
  • 8. Ideal and non-ideal solutions (p. 146)
  • Ideal gases
  • Thermodynamics of ideal gases
  • Ideal solutions
  • Thermodynamics of ideal solutions
  • Dilute solutions
  • Non-ideal solutions
  • Thermodynamics of non-ideal solutions: effective concentrations and activity coefficients
  • Non-ideality in aqueous ionic solutions
  • Debye-Huckel theory
  • Comparison of the Debye--Huckel theory with experiment
  • Concentrated ionic solutions
  • Solutions of uncharged solutes
  • Properties of non-ideal solutions
  • Further reading
  • Problems
  • The Rates of Chemical Reactions
  • 9. Basic chemical kinetics and single-step reactions (p. 171)
  • Kinetics and thermodynamics
  • Energy profiles
  • Empirical observations
  • Reaction rate theories
  • Order and molecularity
  • Reaction half-times
  • Experimental determination of reaction orders and rate constants
  • Effect of temperature on the rate of a reaction
  • Effect of ionic strength on the rate of a reaction
  • Effect of isotopic substitution on the rate of a reaction
  • Further reading
  • Problems
  • 10. Applications of chemical kinetics to multistep reactions (p. 197)
  • Parallel reactions
  • Reversible reactions
  • Consecutive reactions
  • The rate-determining step in consecutive reactions
  • The steady-state approximation in consecutive reactions
  • Effect of pH on the rate of a reaction
  • Further reading
  • Problems
  • 11. Catalysis and enzyme kinetics (p. 213)
  • Catalysis of chemical reactions
  • Enzymes
  • Use of binding energy in catalysing single-substrate reactions
  • Kinetics of single-substrate enzyme reactions
  • Discussion of the Michaelis-Menten equation
  • Enzyme activities
  • Analysis of kinetic data
  • Complications to the basic rate equation
  • Effect of temperature on enzymecatalysed reactions
  • Effect of pH on enzyme-catalysed reactions
  • Further reading
  • Problems
  • 12. Multisubstrate enzyme kinetics and enzyme inhibition (p. 237)
  • Use of binding energy in catalysing multisubstrate reactions
  • Kinetics and mechanisms of two-substrate enzyme reactions
  • Enzyme inhibition
  • Mechanistic implications of inhibitor kinetics
  • Rate equations for inhibition of single-substrate enzyme reactions
  • Further reading
  • Problems
  • 13. Coupled reactions and biochemical pathways (p. 257)
  • Sequential coupling of chemical reactions
  • Parallel coupling of chemical reactions
  • Coupled reactions and biochemical pathways
  • Kinetic control of biochemical pathways
  • The need for a systems-based analysis of kinetic control
  • Metabolic control analysis
  • Control coefficients
  • Elasticities
  • Further reading
  • Problems
  • Atomic and Molecular Structure
  • 14. Quantum mechanics: particles, waves and the quantisation of energy (p. 275)
  • The classical picture of matter and energy
  • Breakdown of the classical picture
  • The wave-particle duality and wave-packets
  • Consequences of the wave-packet nature of matter
  • Localising waves in space gives quantisation of energy
  • Quantisation of energy in molecules
  • Occupancy of energy levels
  • Further reading
  • Problems
  • 15. Electrons in atoms (p. 291)
  • Classical picture of an atom
  • Wave-theory model of an atom
  • Allowed electron orbitals and quantum numbers
  • Electron spin
  • Pauli exclusion principle
  • Electron energies
  • Electronic configurations of atoms and ions
  • Atomic and ionic properties
  • Further reading
  • Problems
  • 16. Bonding in molecules (p. 304)
  • Definition of bonding
  • Types of molecular bonding
  • Electrons in molecules
  • d orbitals in transition metal complexes
  • d-orbital ground-state electronic configurations
  • Valence electron bonding in molecules
  • Properties of molecular bonds
  • Bonding in heteronuclear molecules
  • Bonding in multi-atom molecules
  • Further reading
  • Problems
  • 17. Interaction of molecules with electromagnetic radiation (p. 325)
  • Nature of electromagnetic radiation
  • Absorption of electromagnetic radiation by matter
  • Fate of excited atoms or molecules
  • Basics of spectroscopy
  • Interpreting spectra
  • Further reading
  • Problems
  • 18. Non-covalent interactions and macromolecular structure (p. 340)
  • Non-covalent interactions between atoms
  • Calculating the energies of molecules
  • The role of solvent interactions
  • The hydrophobic effect
  • Thermodynamic stability of structured macromolecules
  • Cooperativity of macromolecular folding and unfolding
  • Further reading
  • Problems
  • Appendices
  • Appendix 1. Note on units and constants (p. 361)
  • Appendix 2. Mathematical tools needed for this text (p. 363)
  • Appendix 3. Answers to problems (p. 367)
  • Index (p. 397)

Author notes provided by Syndetics

Nicholas Price is Professor of Protein Science in the Division of Biochemistry and Molecular Biology, University of Glasgow
Raymond Dwek, FRS, is Head of the Department of Biochemistry and Director of the Glycobiology Institute, University of Oxford and a Professorial Fellow of Exeter College, Oxford
George Ratcliffe is Professor of Plant Sciences in the Department of Plant Sciences, University of Oxford and a Fellow of New College, Oxford
Mark Wormald is a University Research Lecturer in the Glycobiology Institute, Department of Biochemistry, University of Oxford and a Fellow of Corpus Christi College, Oxford