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Descripción

Protein Physics: A Course of Lectures covers the most general problems of protein structure, folding and function. It describes key experimental facts and introduces concepts and theories, dealing with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states.

The book systematically summarizes and presents the results of several decades of worldwide fundamental research on protein physics, structure, and folding, describing many physical models that help readers make estimates and predictions of physical processes that occur in proteins.

New to this revised edition is the inclusion of novel information on amyloid aggregation, natively disordered proteins, protein folding in vivo, protein motors, misfolding, chameleon proteins, advances in protein engineering & design, and advances in the modeling of protein folding.

Further, the book provides problems with solutions, many new and updated references, and physical and mathematical appendices. In addition, new figures (including stereo drawings, with a special appendix showing how to use them) are added, making this an ideal resource for graduate and advanced undergraduate students and researchers in academia in the fields of biophysics, physics, biochemistry, biologists, biotechnology, and chemistry.

  • Fully revised and expanded new edition based on the latest research developments in protein physics
  • Written by the world's top expert in the field
  • Deals with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states
  • Summarizes, in a systematic form, the results of several decades of worldwide fundamental research on protein physics and their structure and folding
  • Examines experimental data on protein structure in the post-genome era

1. Part I: Introduction - p. xx 2. Lecture 1 - p. 3 3. Part II: Elementary Interactions in and Around Proteins - p. 13 4. Lecture 2 - p. 17 5. Lecture 3 - p. 27 6. Lecture 4 - p. 39 7. Lecture 5 - p. 51 8. Lecture 6 - p. 67 9. Part III: Secondary Structures of Polypeptide Chains - p. 82 10. Lecture 7 - p. 85 11. Lecture 8 - p. 101 12. Lecture 9 - p. 123 13. Lecture 10 - p. 139 14. Part IV: Protein Structures - p. 147 15. Lecture 11 - p. 151 16. Lecture 12 - p. 165 17. Lecture 13 - p. 181 18. Lecture 14 - p. 199 19. Lecture 15 - p. 215 20. Lecture 16 - p. 233 21. Part V: Cooperative Transitions in Protein Molecules - p. 250 22. Lecture 17 - p. 253 23. Lecture 18 - p. 275 24. Lecture 19 - p. 289 25. Lecture 20 - p. 307 26. Lecture 21 - p. 323 27. Part VI: Prediction and Design of Protein Structure - p. 346 28. Lecture 22 - p. 349 29. Lecture 23 - p. 367 30. Part VII: Physical Background of Protein Functions - p. 383 31. Lecture 24 - p. 387 32. Lecture 25 - p. 409 33. Appendices - p. 429 34. Problems With Solutions and Comments - p. 457 35. Index - p. 501

Descripcion
Descripción

Protein Physics: A Course of Lectures covers the most general problems of protein structure, folding and function. It describes key experimental facts and introduces concepts and theories, dealing with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states.

The book systematically summarizes and presents the results of several decades of worldwide fundamental research on protein physics, structure, and folding, describing many physical models that help readers make estimates and predictions of physical processes that occur in proteins.

New to this revised edition is the inclusion of novel information on amyloid aggregation, natively disordered proteins, protein folding in vivo, protein motors, misfolding, chameleon proteins, advances in protein engineering & design, and advances in the modeling of protein folding.

Further, the book provides problems with solutions, many new and updated references, and physical and mathematical appendices. In addition, new figures (including stereo drawings, with a special appendix showing how to use them) are added, making this an ideal resource for graduate and advanced undergraduate students and researchers in academia in the fields of biophysics, physics, biochemistry, biologists, biotechnology, and chemistry.

  • Fully revised and expanded new edition based on the latest research developments in protein physics
  • Written by the world's top expert in the field
  • Deals with fibrous, membrane, and water-soluble globular proteins, in both their native and denatured states
  • Summarizes, in a systematic form, the results of several decades of worldwide fundamental research on protein physics and their structure and folding
  • Examines experimental data on protein structure in the post-genome era

1. Part I: Introduction - p. xx 2. Lecture 1 - p. 3 3. Part II: Elementary Interactions in and Around Proteins - p. 13 4. Lecture 2 - p. 17 5. Lecture 3 - p. 27 6. Lecture 4 - p. 39 7. Lecture 5 - p. 51 8. Lecture 6 - p. 67 9. Part III: Secondary Structures of Polypeptide Chains - p. 82 10. Lecture 7 - p. 85 11. Lecture 8 - p. 101 12. Lecture 9 - p. 123 13. Lecture 10 - p. 139 14. Part IV: Protein Structures - p. 147 15. Lecture 11 - p. 151 16. Lecture 12 - p. 165 17. Lecture 13 - p. 181 18. Lecture 14 - p. 199 19. Lecture 15 - p. 215 20. Lecture 16 - p. 233 21. Part V: Cooperative Transitions in Protein Molecules - p. 250 22. Lecture 17 - p. 253 23. Lecture 18 - p. 275 24. Lecture 19 - p. 289 25. Lecture 20 - p. 307 26. Lecture 21 - p. 323 27. Part VI: Prediction and Design of Protein Structure - p. 346 28. Lecture 22 - p. 349 29. Lecture 23 - p. 367 30. Part VII: Physical Background of Protein Functions - p. 383 31. Lecture 24 - p. 387 32. Lecture 25 - p. 409 33. Appendices - p. 429 34. Problems With Solutions and Comments - p. 457 35. Index - p. 501

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