UID:
almafu_9960072250302883
Format:
1 online resource (421 p.)
ISBN:
1-281-02318-3
,
9786611023188
,
0-08-052452-4
Series Statement:
Advances in protein chemistry, v. 62
Content:
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* Detec
Note:
Description based upon print version of record.
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Front Cover; Unfolded Proteins; Copyright Page; CONTENTS; John T. Edsall And Advances In Protein Chemistry; Getting To Know U; John T. Edsall; Chapter 1. The Expanded Denatured State: An Ensemble of Conformations Trapped in a Locally Encoded Topological Space; I. Introduction; II. Nuclease 131: Local Structure; III. Nuclease 131: Long-Range Structure; IV. Physical-Chemical Explanations of Long-Range Structure; V. Conclusions; References; Chapter 2. Identification and Functions of Usefully Disordered Proteins; I. Testing Whether Intrinsic Disorder Is Encoded by the Amino Acid Sequence
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II. Prediction of Order and Disorder from the Amino Acid SequenceIII. PONDR Estimations of the Commonness of Intrinsically Disordered Proteins; IV. Functions of Intrinsically Disordered Regions; V. Conclusions; References; Chapter 3. Unfolded Proteins Studied by Raman Optical Activity; I. Introduction; II. Raman Optical Activity Theory and Experiment; III. Survey of Polypeptide and Protein Raman Optical Activity; IV. Unfolded Proteins; V. Principal Component Analysis; VI. Concluding Remarks; References; Chapter 4. What Fluorescence Correlation Spectroscopy Can Tell Us about Unfolded Proteins
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I. IntroductionII. Fluorescence Correlation Spectroscopy Technique and Theory; III. Application to Conformational Changes within the Unfolded State; IV. Advantages and Disadvantages of Using Fluorescence Correlation Spectroscopy to Study Protein Conformational Changes; V. Experimental Studies; VI. Concluding Remarks; References; Chapter 5. Unfolded Peptides and Proteins Studied with Infrared Absorption and Vibrational Circular Dichroism Spectra; I. Introduction; II. Experimental Techniques; III. Theoretical Simulation of IR and VCD Spectra; IV. Peptide Studies; V. Protein Studies
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VI. ConclusionReferences; Chapter 6. Is Polyproline II a Major Backbone Conformation in Unfolded Proteins?; I. Introduction; II. Polyproline II Dominates in Short Peptides; III. Circular Dichroism of Unfolded Proteins; IV. Summary and Broader Implications; References; Chapter 7. Toward a Taxonomy of the Denatured State: Small Angle Scattering Studies of Unfolded Proteins; I. Introduction; II. A Taxonomy of Unfolded States; III. A Random-Coil Denatured State?; IV. Reconciling the Random Coil with a Structured Denatured State; References
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Chapter 8. Determinants of the Polyproline II Helix from Modeling StudiesI. Introduction; II. The Left-Handed Polyproline II Conformation; III. Physical Determinants of the Polyproline II Conformation; IV. Surveys of Known Protein Structures; V. Modeling Studies of Polyproline II Helix Determinants; VI. Summary; References; Chapter 9. Hydration Theory for Molecular Biophysics; I. Introduction; II. Potential Distribution Theorem and Preliminaries; III. Applications of the Potential Distribution Theorem; IV. The Potential Distribution Theorem Revisited; V. Quasi-Chemical Theory of Solutions
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VI. Primitive Quasi-Chemical Approximation
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English
Additional Edition:
ISBN 0-12-034262-6
Language:
English
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