Unfolded Proteins
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Table of contents
- Copyright Pageiv
- Contentsv
- John T. Edsall And Advances In Protein Chemistryxi
- Getting To Know Uxv
- John T. Edsallxxiii
- Chapter 1. The Expanded Denatured State: An Ensemble of Conformations Trapped in a Locally Encoded T1
- I. Introduction1
- II. Nuclease 131: Local Structure4
- III. Nuclease 131: Long-Range Structure9
- IV. Physical-Chemical Explanations of Long-Range Structure14
- V. Conclusions19
- References22
- Chapter 2. Identification and Functions of Usefully Disordered Proteins25
- I. Testing Whether Intrinsic Disorder Is Encoded by the Amino Acid Sequence26
- II. Prediction of Order and Disorder from the Amino Acid Sequence37
- III. PONDR Estimations of the Commonness of Intrinsically Disordered Proteins42
- IV. Functions of Intrinsically Disordered Regions45
- V. Conclusions46
- References46
- Chapter 3. Unfolded Proteins Studied by Raman Optical Activity51
- I. Introduction51
- II. Raman Optical Activity Theory and Experiment54
- III. Survey of Polypeptide and Protein Raman Optical Activity59
- IV. Unfolded Proteins68
- V. Principal Component Analysis84
- VI. Concluding Remarks86
- References86
- Chapter 4. What Fluorescence Correlation Spectroscopy Can Tell Us about Unfolded Proteins91
- I. Introduction91
- II. Fluorescence Correlation Spectroscopy Technique and Theory93
- III. Application to Conformational Changes within the Unfolded State100
- IV. Advantages and Disadvantages of Using Fluorescence Correlation Spectroscopy to Study Protein Con101
- V. Experimental Studies103
- VI. Concluding Remarks108
- References109
- Chapter 5. Unfolded Peptides and Proteins Studied with Infrared Absorption and Vibrational Circular111
- I. Introduction111
- II. Experimental Techniques118
- III. Theoretical Simulation of IR and VCD Spectra123
- IV. Peptide Studies125
- V. Protein Studies138
- VI. Conclusion154
- References155
- Chapter 6. Is Polyproline II a Major Backbone Conformation in Unfolded Proteins?163
- I. Introduction163
- II. Polyproline II Dominates in Short Peptides164
- III. Circular Dichroism of Unfolded Proteins198
- IV. Summary and Broader Implications228
- References233
- Chapter 7. Toward a Taxonomy of the Denatured State: Small Angle Scattering Studies of Unfolded Prot241
- I. Introduction241
- II. A Taxonomy of Unfolded States242
- III. A Random-Coil Denatured State?254
- IV. Reconciling the Random Coil with a Structured Denatured State257
- References259
- Chapter 8. Determinants of the Polyproline II Helix from Modeling Studies263
- I. Introduction263
- II. The Left-Handed Polyproline II Conformation265
- III. Physical Determinants of the Polyproline II Conformation266
- IV. Surveys of Known Protein Structures267
- V. Modeling Studies of Polyproline II Helix Determinants273
- VI. Summary280
- References281
- Chapter 9. Hydration Theory for Molecular Biophysics283
- I. Introduction283
- II. Potential Distribution Theorem and Preliminaries286
- III. Applications of the Potential Distribution Theorem289
- IV. The Potential Distribution Theorem Revisited297
- V. Quasi-Chemical Theory of Solutions299
- VI. Primitive Quasi-Chemical Approximation304
- VII. Conclusions307
- References308
- Chapter 10. Insights into the Structure and Dynamics of Unfolded Proteins from Nuclear Magnetic Reso311
- I. Introduction311
- II. Conformational Propensities in Peptides312
- III. NMR Studies of Unfolded and Partly Folded Proteins313
- IV. Insights into Structure and Dynamics of Unfolded States324
- V. Conclusions337
- References337
- Chapter 11. Unfolded State of Peptides341
- I. Introduction341
- II. Definitions343
- III. A Sample of Unfolded States344
- IV. Epilogue357
- References357
- Chapter 12. A New Perspective on Unfolded Proteins361
- I. Introduction361
- II. Hydrophobic Clusters in Urea-Denatured Proteins362
- III. Rationale for Studying Denatured Proteins in Water362
- IV. Stiffness of the Random Chain363
- V. Preferred Backbone Conformations364
- References366
- AUTHOR INDEX369
- SUBJECT INDEX389
A variety of complementary techniques and approaches have been used to characterize peptide and protein unfolding induced by temperature, pressure, and solvent. Volume 62, Unfolded Proteins, assembles these complementary views to develop a more complete picture of denatured peptides and proteins. The unifying observation common to all chapters is the detection of preferred backbone confirmations in experimentally accessible unfolded states.
Key Features
* Peptide and protein unfolding induced by temperature, pressure, and solvent
* Denatured peptides and proteins
* Detection of preferred backbone confirmations in experimentally accessible unfolded states
Key Features
* Peptide and protein unfolding induced by temperature, pressure, and solvent
* Denatured peptides and proteins
* Detection of preferred backbone confirmations in experimentally accessible unfolded states