Download e-book for iPad: Mass Spectrometry in Structural Biology and Biophysics: by Igor A. Kaltashov, Stephen J. Eyles(auth.), Dominic M.

By Igor A. Kaltashov, Stephen J. Eyles(auth.), Dominic M. Desiderio, Nico M. M. Nibbering(eds.)

ISBN-10: 0470937793

ISBN-13: 9780470937792

ISBN-10: 1118232127

ISBN-13: 9781118232125

Content material:
Chapter 1 common evaluate of easy techniques in Molecular Biophysics (pages 1–25):
Chapter 2 evaluation of conventional Experimental Arsenal to check Biomolecular constitution and Dynamics (pages 26–51):
Chapter three assessment of organic Mass Spectrometry (pages 52–88):
Chapter four Mass Spectrometry established techniques to review Biomolecular larger Order constitution (pages 89–126):
Chapter five Mass Spectrometry established techniques to review Biomolecular Dynamics: Equilibrium Intermediates (pages 127–159):
Chapter 6 Kinetic experiences via Mass Spectrometry (pages 160–185):
Chapter 7 Protein Interactions: a more in-depth examine the Structure–Dynamics–Function Triad (pages 186–211):
Chapter eight different Biopolymers and artificial Polymers of organic curiosity (pages 212–238):
Chapter nine Mass Spectrometry at the Frontiers of Molecular Biophysics and Structural Biology: views and demanding situations (pages 239–278):

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Extra info for Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules, Second Edition

Example text

Several new concepts have been introduced to reflect the structural diversity and dynamic character of the molten globule state, 13 such as “a precursor of the molten globule” and “a highly structured molten globule” (57). One common question that arises is whether the equilibrium molten globule intermediate is actually the same species as that detected in the folding pathway of proteins. Thermodynamically there is nothing to suggest they should be, since the equilibrium by definition is independent of the pathway (58,59).

31. Rost, B. (1997) Protein structures sustain evolutionary drift, Fold. Des. 2, S19–S24. 32. Wood, T. C. and Pearson, W. R. (1999) Evolution of protein sequences and structures, J. Mol. Biol. 291, 977–995. 33. Zhang, C. and DeLisi, C. (2001) Protein folds: molecular systematics in three dimensions, Cell. Mol. Life Sci. 58, 72–79. 34. Denton, M. , Marshall, C. , and Legge, M. (2002) The protein folds as platonic forms: New support for the 35. 36. 37. 38. 39. 40. 41. 42. 43. 44. 45. 46. 47. 48. 49.

8, 68–79. 72. Bryngelson, J. , Onuchic, J. , Socci, N. , and Wolynes, P. G. , Proteins 21, 167–195. 73. Onuchic, J. , and Wolynes, P. G. (1997) Theory of protein folding: the energy landscape perspective, Annu. Rev. Phys. Chem. 48, 545–600. 74. Brooks, C. , Onuchic, J. , and Wolynes, P. _G. (1998) Chemical physics of protein folding, Proc. Natl. Acad. Sci. USA 95, 11037–11038. 75. Plotkin, S. S. and Onuchic, J. N. (2002) Understanding protein folding with energy landscape theory. Part I: Basic concepts, Q.

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Mass Spectrometry in Structural Biology and Biophysics: Architecture, Dynamics, and Interaction of Biomolecules, Second Edition by Igor A. Kaltashov, Stephen J. Eyles(auth.), Dominic M. Desiderio, Nico M. M. Nibbering(eds.)


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