
Physical Chemistry
Principles and Applications in Biological Sciences
Ignacio, Jr. Tinoco, Kenneth Sauer, James C. Wang, Joseph D. Puglisi
Résumé
Features
An enhanced pedagogical focus this edition.
- NEW—Improved chapter-end problems—This has always been a strength of this text, but now essentially all of the end-of-chapter problems are biologically relevant.
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- Presents assessment material in a relevant context.
- NEW—Updated and expanded references and suggested readings.
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- Makes this a useful reference text.
- NEW—Clearer, more explicit writing—Explains the important equations in words.
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- Helps the students, especially those with weaker math skills, cement their conceptual understanding of physical chemistry.
- Mathematics at an appropriate level.
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- Uses elementary calculus to derive equations but does not require students to know it to solve problems.
Scope of content refined and updated to reflect new advances in and applications of physical chemistry.
- NEW—New applications—e.g., single-molecule experiments.
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- Engages students by introducing them to the latest physical chemistry important in biochemistry and molecular biology.
- NEW—Enhanced emphasis on methods that are important in biology—e.g., fluorescence.
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- Introduces students to techniques that are important in biochemistry and molecular biology.
- NEW—Includes a new section on biological membranes—Strengthened descriptions of lipids, the formation of micelles, vesicles and bilayers and the relation to surface tension.
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- Improves the coverage in this biologically important area. Ex. Chapter 5.
- NEW—Theory of molecular structure and interactions—Ch. 9 now begins with the origins of quantum mechanics, and builds up to intermolecular and intramolecular forces and the use of semi-empirical methods to calculate molecular conformations.
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- Gives students a better understanding of the foundations of the concepts and methods used to calculate and predict macromolecular structures.
- NEW—Ch. 10 has an increased emphasis on nuclear magnetic resonance and fluorescence spectroscopy—Nuclear magnetic resonance and fluorescence are the two main methods used to study proteins and nucleic acids in solution. The increased emphasis mirrors this fact.
- NEW—Ch. 11 has more specific examples of statistical weights in ligand binding.
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- Helps students understand hormone and drug binding to receptors.
- NEW—Molecular structures and X-ray diffraction are now in Ch. 12—Provides a more detailed discussion of how a structure is obtained from a measured diffraction pattern.
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- X-ray diffraction is now available to non-specialists to determine structures of proteins and nucleic acids. Students need to learn how this is done.
Contents
- 1. Introduction.
- 2. The First Law: Energy Is Conserved.
- 3. The Second Law: The Entropy of the Universe Increases.
- 4. Free Energy and Chemical Equilibria.
- 5. Free Energy and Physical Equilibria.
- 6. Molecular Motion and Transport Properties.
- 7. Kinetics: Rates of Chemical Reactions.
- 8. Enzyme Kinetics.
- 9. Molecular Structures and Interactions: Theory.
- 10. Molecular Structures and Interactions: Spectroscopy.
- 11. Molecular Distributions and Statistical Thermodynamics.
- 12. Macromolecular Structure and X-Ray Diffraction.
- Appendix.
- Answers to Selected Problems.
- Index.
Caractéristiques techniques
PAPIER | |
Éditeur(s) | Prentice Hall |
Auteur(s) | Ignacio, Jr. Tinoco, Kenneth Sauer, James C. Wang, Joseph D. Puglisi |
Parution | 01/09/2001 |
Édition | 4eme édition |
Nb. de pages | 740 |
Format | 21 x 26 |
Couverture | Relié |
Poids | 1570g |
Intérieur | Noir et Blanc |
EAN13 | 9780130959430 |
ISBN13 | 978-0-13-095943-0 |
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