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Biothermodynamics, Part D, Volume 492 [Kietas viršelis]

Volume editor (University of Virginia Health Sciences Center, Charlottesville, USA), Volume editor (Washington University School of Medicine, St. Louis, Mo, USA), Volume editor (Washington University Medical Center, St. Louis, MO, USA)
  • Formatas: Hardback, 369 pages, aukštis x plotis: 229x152 mm, weight: 750 g
  • Serija: Methods in Enzymology
  • Išleidimo metai: 05-Apr-2011
  • Leidėjas: Academic Press Inc
  • ISBN-10: 0123860032
  • ISBN-13: 9780123860033
Kitos knygos pagal šią temą:
  • Formatas: Hardback, 369 pages, aukštis x plotis: 229x152 mm, weight: 750 g
  • Serija: Methods in Enzymology
  • Išleidimo metai: 05-Apr-2011
  • Leidėjas: Academic Press Inc
  • ISBN-10: 0123860032
  • ISBN-13: 9780123860033
Kitos knygos pagal šią temą:
The use of thermodynamics in biological research can be equated to an energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. This volume presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions.

* Elucidates the relationships between structure and energetics and their applications to molecular design, aiding researchers in the design of medically important molecules * Provides a "must-have" methods volume that keeps MIE buyers and online subscribers up-to-date with the latest research * Offers step-by-step lab instructions, including necessary equipment, from a global research community

Daugiau informacijos

This volume presents robust and modern thermodynamic methods for determining the functional energetics of macromolecular structures with their biological functions.
Contributors ix
Preface xiii
Volumes in Series xv
1 A Thermodynamic Approach for the Targeting of Nucleic Acid Structures Using Their Complementary Single Strands
1(26)
Hui-Ting Lee
Caroline Carr
Hollie Siebler
Lela Waters
Irine Khutsishvili
Fany Iseka
Brian Domack
Chris M. Olsen
Luis A. Marky
1 Introduction
2(2)
2 Materials and Methods
4(4)
3 Results and Discussion
8(15)
4 Conclusions
23(1)
Acknowledgments
24(1)
References
24(3)
2 Thermodynamics of Biological Processes
27(34)
Hernan G. Garcia
Jane Kondev
Nigel Orme
Julie A. Theriot
Rob Phillips
1 Introduction: Thermodynamics is Not Just for Dead Stuff
28(1)
2 States and Weights from the Boltzmann Rule
29(4)
3 Binding Reactions and Biological Thermodynamics
33(19)
4 The Unreasonable Effectiveness of Random-Walk Models
52(3)
5 Conclusions
55(1)
Acknowledgments
56(1)
References
56(5)
3 Protein Stability in the Presence of Cosolutes
61(66)
Luis Marcelo F. Holthauzen
Matthew Auton
Mikhail Sinev
Jorg Rosgen
1 Introduction
62(2)
2 Isothermal Folding/Unfolding of Protein in the Presence of Stabilizing/Denaturing Osmolyte
64(14)
3 Isothermal Protein (Un)Folding in the Presence of Osmolyte Mixtures
78(8)
4 Osmolyte-Induced Unfolding at Variable Temperature
86(6)
5 Thermal Unfolding in the Presence of Osmolytes
92(9)
6 Where Do the Little Equations Come From?
101(20)
Acknowledgment
121(1)
References
121(6)
4 Small-Angle X-ray Scattering Studies of Peptide-Lipid Interactions Using the Mouse Paneth Cell α-Defensin Cryptdin-4
127(24)
Abhijit Mishra
Kenneth P. Tai
Nathan W. Schmidt
Andre J. Ouellette
Gerard C. L. Wong
1 Introduction
128(4)
2 X-Rays as Structural Probes of Biological Systems Under Biomimetic Conditions
132(5)
3 Preparation of Peptide-Lipid Complexes for X-Ray Measurements
137(8)
4 Summary
145(1)
Acknowledgments
145(1)
References
145(6)
5 Synergy of Molecular Dynamics and Isothermal Titration Calorimetry in Studies of Allostery
151(38)
Rebecca Strawn
Thomas Stockner
Milan Melichercik
Lihua Jin
Wei-Feng Xue
Jannette Carey
Rudiger Ettrich
1 Allostery
152(2)
2 Arginine Repressor
154(3)
3 Preparation for Simulations
157(2)
4 Sampling of States
159(1)
5 Equilibration
160(3)
6 Observing System Motions
163(1)
7 Correlated Motions
163(1)
8 Structural Features of Correlated Motions
164(3)
9 Arg Residues Promote Rotation and Oscillation
167(2)
10 Structural Correlates of Rotational Oscillation
169(1)
11 Single-Arginine Simulations
169(1)
12 Rotational Ensembles
170(3)
13 Energetic Contributions
173(4)
14 Reconciliation with Crystallographic Data
177(2)
15 Complementarity and Synergy of MD and ITC
179(5)
16 Prospects
184(2)
Acknowledgement
186(1)
References
186(3)
6 Using Tryptophan Fluorescence to Measure the Stability of Membrane Proteins Folded in Liposomes
189(24)
C. Preston Moon
Karen G. Fleming
1 Introduction
190(1)
2 Issues with Managing Light Scattering from Liposomes
191(9)
3 Using Tryptophan Spectral Properties to Monitor Membrane Protein Folding into Liposomes
200(5)
4 Choosing an Appropriate Tryptophan Spectral Property to Measure the Thermodynamic Stabilities of Folded Membrane Proteins
205(2)
5 Conclusions
207(2)
6 Materials and Methods
209(1)
Acknowledgments
210(1)
References
210(3)
7 Non-B Conformations of CAG Repeats Using 2-Aminopurine
213(20)
Natalya N. Degtyareva
Jeffrey T. Petty
1 Introduction
214(2)
2 Materials and Methods
216(7)
3 Structure and Thermodynamics of Isolated and Integrated (CAG)8
223(6)
4 Conclusions
229(1)
Acknowledgments
229(1)
References
229(4)
8 Disulfide Bond-Mediated Passenger Domain Stalling as a Structural Probe of Autotransporter Outer Membrane Secretion In Vivo
233(20)
Jonathan P. Renn
Patricia L. Clark
1 Protein Secretion: An Essential Component of Bacterial Virulence
234(1)
2 The Autotransporter Secretion Pathway
234(2)
3 Overview of Cys-Loop Stalling
236(1)
4 Architecture and Processing of AT Passenger Domains
236(3)
5 Heterologous Passenger Domain Secretion
239(1)
6 Selecting a Model Autotransporter for Cys-Loop Stalling
240(1)
7 Disulfide Mediated Passenger Domain Stalling
241(3)
8 Methods to Measure OM Secretion and Folding of the Stalled AT Passenger
244(4)
9 Applications: Using Cys-Loop Stalling to Define the Mechanism of AT OM Secretion
248(1)
References
249(4)
9 Strategies for the Thermodynamic Characterization of Linked Binding/Local Folding Reactions Within the Native State: Application to the LID Domain of Adenylate Kinase from Escherichia coli
253(30)
Travis P. Schrank
W. Austin Elam
Jing Li
Vincent J. Hilser
1 Introduction
254(2)
2 A Mutation Strategy to Amplify Locally Unfolded States
256(4)
3 Thermodynamic Properties of Linked Folding and Binding Reactions
260(5)
4 Strategies for Quantitative Interpretation of Measured Enthalpies for a Linked Folding and Binding System
265(3)
5 Interplay of Local Mutational Effects, Global Stability, and Binding Affinity
268(5)
6 Success of the Strategy in Preserving Structure
273(1)
7 Comparison of Interaction Versus Entropy Based Mutation Strategy
274(2)
8 How Similar Are Local and Global Unfolding?
276(3)
9 Summary
279(1)
References
280(3)
10 Fluorescence-Detected Sedimentation in Dilute and Highly Concentrated Solutions
283(22)
Jonathan S. Kingsbury
Thomas M. Laue
1 Overview of AUC
284(1)
2 Fluorescence Optics for the Ultracentrifuge
285(2)
3 Advantages of AU-FDS
287(1)
4 Sample Requirements for Fluorescence Detection
288(5)
5 Applications of AU-FDS
293(5)
6 Current Challenges for AU-FDS
298(3)
7 Conclusion
301(1)
References
302(3)
Author Index 305(12)
Subject Index 317