Preface |
|
vii | |
Editors |
|
ix | |
Contributors |
|
xi | |
|
PART I Pulling on Single Molecules with Force Spectroscopy |
|
|
|
Chapter 1 Molecular Recognition Force Spectroscopy |
|
|
3 | (44) |
|
|
|
|
|
|
|
|
|
1.1 Single-Molecule Force Spectroscopy |
|
|
4 | (10) |
|
|
4 | (3) |
|
1.1.2 Dynamic Single-Molecule Force Spectroscopy and Molecular Recognition |
|
|
7 | (2) |
|
1.1.3 Surface Chemistry for Single-Molecule Studies |
|
|
9 | (1) |
|
|
10 | (3) |
|
1.1.3.2 Substrate Preparation |
|
|
13 | (1) |
|
1.2 Molecular Recognition Force Spectroscopy on Synthetic Host-Guest Systems |
|
|
14 | (3) |
|
1.3 Molecular Recognition Force Spectroscopy on Biological Systems |
|
|
17 | (7) |
|
|
17 | (1) |
|
|
18 | (1) |
|
1.3.2.1 Nuclear Pore Complexes |
|
|
18 | (1) |
|
|
19 | (3) |
|
1.3.2.3 Human Rhinovirus and Cells |
|
|
22 | (2) |
|
1.4 Molecular Recognition Mapping Using Force Spectroscopy |
|
|
24 | (3) |
|
1.5 Simultaneous Dynamic Imaging of Topography and Recognition |
|
|
27 | (9) |
|
|
27 | (3) |
|
|
30 | (1) |
|
1.5.2.1 Bacterial Surface Layers |
|
|
30 | (2) |
|
1.5.2.2 Human Red Blood Cell Membranes |
|
|
32 | (1) |
|
|
33 | (3) |
|
|
36 | (1) |
|
|
36 | (11) |
|
Chapter 2 Mechanics of Proteins and Tailored Mechanics of Engineered Proteins |
|
|
47 | (36) |
|
|
|
|
2.1 A Brief Introduction: The Utility of Investigating Protein Mechanics on the Single-Molecule Scale |
|
|
48 | (2) |
|
2.2 Use of Force Spectroscopy to Explicate Nanomechanical Properties of Protein |
|
|
50 | (10) |
|
2.2.1 First Single-Molecule AFM Protein Studies |
|
|
50 | (1) |
|
2.2.2 Representing Protein Mechanical Stability Using Single-Molecule AFM |
|
|
50 | (2) |
|
2.2.3 Constructing Polyprotein to Pinpoint the Nanomechanics of Protein Domains of Interest |
|
|
52 | (1) |
|
2.2.4 How Applied Force Unfolds a Protein |
|
|
53 | (1) |
|
2.2.5 Mechanical Stability: A Kinetic, rather than Thermodynamic, Stability |
|
|
54 | (1) |
|
2.2.6 Constructing the Free Energy Landscape for Protein Unfolding from Single-Molecule AFM Experiments |
|
|
55 | (3) |
|
2.2.7 Structural Features of Proteins Obtained from Force-Extension Spectrum |
|
|
58 | (1) |
|
2.2.8 Unfolding Force Depends on Pulling Direction: The Importance of Local Structure to the Mechanical Stability of Proteins |
|
|
59 | (1) |
|
2.3 Tuning the Properties of Proteins: Tailoring Protein Mechanics for Use with Single-Molecule AFM |
|
|
60 | (14) |
|
2.3.1 Present Modifications and Their Application with Single-Molecule AFM |
|
|
60 | (1) |
|
2.3.2 Introducing Point Mutations into the Native Protein Backbone: Nanomechanical Effects of Single-Point Mutations |
|
|
61 | (3) |
|
2.3.3 Recombination of Structural Fragments or Structural Grafting |
|
|
64 | (3) |
|
2.3.4 Intramolecular Disulfide Bonding and Loop Insertion |
|
|
67 | (1) |
|
2.3.5 Ligand Binding Modifies the Unfolding Energy Landscape |
|
|
68 | (2) |
|
2.3.6 Investigating the Nanomechanics of a Novel Protein Fold: Top7 |
|
|
70 | (1) |
|
2.3.7 Environmental/Solvent Tuning of Mechanical Stability |
|
|
71 | (2) |
|
2.3.8 Predicting Mechanical Properties Using Modeling Approaches |
|
|
73 | (1) |
|
2.4 Future Perspectives: Rationally Controlling and Designing Proteins with Desired Nanomechanical Properties |
|
|
74 | (2) |
|
2.4.1 Learning from Nature: How Tunable Functionality Originates within Protein Structure |
|
|
74 | (1) |
|
2.4.2 Cracking the Structure/Function Relationship: Further Protein Modifications Investigated Using Single-Molecule AFM |
|
|
75 | (1) |
|
2.4.3 The Future: Rationally Designing Proteins with Desired Functionality |
|
|
75 | (1) |
|
|
76 | (7) |
|
Chapter 3 Mechanics of Polysaccharides |
|
|
83 | (46) |
|
|
|
|
|
|
84 | (3) |
|
3.2 Overview of Polysaccharide Structure |
|
|
87 | (1) |
|
3.3 Overview of Polysaccharide Elasticity |
|
|
88 | (2) |
|
3.4 Atomic Force Spectroscopy of Single Polysaccharides |
|
|
90 | (26) |
|
3.4.1 Experimental Methods |
|
|
90 | (1) |
|
3.4.1.1 Polysaccharides and Their Preparation for AFM Measurements |
|
|
90 | (1) |
|
3.4.1.2 AFM Instruments and the Principles of Single-Molecule Atomic Force Spectroscopy |
|
|
90 | (2) |
|
3.4.1.3 Interpretation of Force-Extension Relationships: Identifying Single-Molecule Force Spectra |
|
|
92 | (1) |
|
3.4.1.4 Normalization of Polysaccharide Extension |
|
|
93 | (1) |
|
3.4.1.5 Pulling Geometry Errors |
|
|
94 | (1) |
|
3.4.2 Basic Computational Approaches for Modeling Sugar Mechanics |
|
|
94 | (1) |
|
3.4.2.1 Quantum Mechanics-Based Methods for Analyzing Strained Sugar Conformations |
|
|
94 | (2) |
|
3.4.2.2 Steered Molecular Dynamics Simulations of Polysaccharide Elasticity |
|
|
96 | (1) |
|
3.4.3 (1→4) Linked Polysaccharides and Their Force-Induced Conformational Transitions |
|
|
97 | (1) |
|
3.4.3.1 Cellulose and Amylose: Force-Induced Chair-Boat Transitions |
|
|
97 | (3) |
|
3.4.3.2 Galactan: Identifying Sugar Isomers by AFM Force Spectroscopy |
|
|
100 | (3) |
|
3.4.3.3 Pectin: Atomic Levers Control Pyranose Ring Conformations |
|
|
103 | (2) |
|
3.4.4 (1→6) Linked Polysaccharides: Atomic Cranks and Levers Control Pyranose Ring Conformations |
|
|
105 | (1) |
|
|
105 | (2) |
|
|
107 | (1) |
|
3.4.5 Molecular Elasticity of Epimerized Polysaccharides |
|
|
108 | (1) |
|
|
109 | (4) |
|
3.4.6 Fingerprinting Polysaccharides with AFM |
|
|
113 | (2) |
|
|
115 | (1) |
|
3.5 Simulations of AFM Experiments for Polysaccharides |
|
|
116 | (7) |
|
3.5.1 Obtaining Fully Converged Results from the Samplings under Equilibrium Conditions: Comparisons of SMD, REM-SMD, REM-US |
|
|
116 | (3) |
|
3.5.2 Latest Simulation Results and Conformational Transitions, Using REM-US and Glycam06 |
|
|
119 | (3) |
|
3.5.3 Comparison of the Application of Classical Force Fields and Quantum Mechanics-Based Methods to Modeling of Polysaccharide Mechanics |
|
|
122 | (1) |
|
|
123 | (1) |
|
|
123 | (1) |
|
|
123 | (6) |
|
Chapter 4 Mechanics and Interactions in DNA and RNA |
|
|
129 | (20) |
|
|
|
129 | (1) |
|
4.2 Protein-DNA Interactions |
|
|
130 | (8) |
|
4.2.1 Interaction of Transcriptional Regulators with DNA Target Sequences |
|
|
130 | (3) |
|
4.2.2 Effector Stimulated Protein-DNA Interactions |
|
|
133 | (2) |
|
4.2.3 Improved Model for the Data Analysis |
|
|
135 | (3) |
|
4.3 Protein-RNA Interactions |
|
|
138 | (3) |
|
4.4 Binding of Small Molecules to dsDNA |
|
|
141 | (4) |
|
4.5 Conclusion and Outlook |
|
|
145 | (1) |
|
|
146 | (3) |
|
Chapter 5 Mechanics of Synthetic Polymers |
|
|
149 | (16) |
|
|
|
|
5.1 Effect of Chain Composition on the Elasticity of Synthetic Single Polymers |
|
|
150 | (6) |
|
|
150 | (2) |
|
5.1.2 Linear Charge Density Effects on the Single Chain Elasticity |
|
|
152 | (1) |
|
5.1.3 Tacticity Effect on Single-Chain Elasticity |
|
|
153 | (1) |
|
5.1.4 Effects of Oxidization/Reduction States on Elasticity |
|
|
154 | (2) |
|
5.2 Interaction of Small Molecule with Polymer |
|
|
156 | (5) |
|
5.2.1 Effects of Urea on Nanomechanics of Poly(Acrylamide) Derivatives |
|
|
156 | (1) |
|
5.2.2 Effect of Water on the Nanomechanics of Poly(Ethylene Glycol) |
|
|
157 | (1) |
|
5.2.3 Binding of Water or KI3 Molecules Changes the Elastic Properties of Poly(N-Vinyl-2-Pyrrolidone) |
|
|
158 | (1) |
|
5.2.4 Nanomechanics of Single Amylose Chains in Crowding Environment |
|
|
159 | (2) |
|
5.3 Aggregating Effect on Nanomechanics of Single Polymer Chain |
|
|
161 | (1) |
|
5.3.1 Force-Induced Globule-Coil Transition in Single Polystyrene Chains |
|
|
161 | (1) |
|
5.3.2 Forces Required to Disassemble the Block Copolymer Micelles of PAA-PF-PAA |
|
|
162 | (1) |
|
|
162 | (3) |
|
Chapter 6 Interplays between Chemistry and Mechanics in Single Molecules |
|
|
165 | (32) |
|
|
|
|
165 | (1) |
|
6.2 Effect of Force on Thermodynamics and Kinetics of a Reaction |
|
|
166 | (5) |
|
6.2.1 Effect of Force on the Free Energy of a Reaction |
|
|
167 | (3) |
|
6.2.2 Effect of Force on the Kinetics of a Reaction |
|
|
170 | (1) |
|
6.3 Single-Molecule Force Spectroscopy |
|
|
171 | (14) |
|
6.3.1 Methodologies for Single-Molecule Force Spectroscopy |
|
|
172 | (2) |
|
6.3.2 Mapping the Position of the Barrier according to the Dynamic Force Spectroscopy Approach |
|
|
174 | (1) |
|
6.3.3 AFM-Based Single-Molecule Force Spectroscopy of GB1 Protein |
|
|
175 | (2) |
|
6.3.4 AFM-Based Single-Molecule Force Spectroscopy of GB1 Protein in the Presence of Chemical Osmolytes |
|
|
177 | (2) |
|
6.3.5 Molecular Engineering of Mechanical Properties |
|
|
179 | (6) |
|
6.4 Mechanochemistry of a Single Covalent Bond |
|
|
185 | (4) |
|
6.4.1 Disulfide Bond Reduction Reactions by Small Nucleophiles |
|
|
185 | (4) |
|
6.5 Mechanochemistry for a Targeted Delivery of Single Molecules |
|
|
189 | (1) |
|
6.6 Conclusion and Prospective |
|
|
190 | (1) |
|
|
190 | (7) |
|
PART II Manipulation, Repositioning, and Targeted Delivery of Single Molecules on Substrates |
|
|
|
Chapter 7 Molecular Construction: Pushing, Moving, Stretching, and Connecting Individual Molecules |
|
|
197 | (12) |
|
|
|
7.1 Moving Single Molecules on Surfaces |
|
|
198 | (1) |
|
7.2 Stretching Single Molecules on Surfaces |
|
|
199 | (4) |
|
7.2.1 Using Contact Mode SFM |
|
|
199 | (2) |
|
7.2.2 Using Intermittent Contact Mode SFM |
|
|
201 | (2) |
|
7.3 Connecting Individual Molecules on Surfaces |
|
|
203 | (2) |
|
|
205 | (1) |
|
|
205 | (1) |
|
|
205 | (4) |
|
Chapter 8 Extracting Molecules from Surfaces |
|
|
209 | (28) |
|
|
|
Takahiro Watanaba-Nakayama |
|
|
|
|
209 | (1) |
|
8.2 Why Extract by Force? |
|
|
210 | (1) |
|
8.3 Preparation for Extraction Experiments |
|
|
211 | (2) |
|
8.4 Extraction of Lipid Molecules |
|
|
213 | (3) |
|
8.5 Pulling Helical Polypeptides from the Lipid Bilayer Membrane |
|
|
216 | (1) |
|
8.6 Extraction of Intrinsic Membrane Proteins |
|
|
217 | (6) |
|
8.7 Proteins with Lipid Tethers |
|
|
223 | (1) |
|
8.8 Retrieval of Genomic DNA from Isolated Chromosomes |
|
|
224 | (3) |
|
8.9 Retrieval of Intracellular mRNA |
|
|
227 | (1) |
|
8.10 Creating Membrane Holes Using AFM Probes |
|
|
228 | (5) |
|
8.11 Conclusions and Future Prospects |
|
|
233 | (1) |
|
|
234 | (1) |
|
|
234 | (3) |
|
Chapter 9 Single-Molecule Delivery by Mechanochemistry |
|
|
237 | (12) |
|
|
|
|
246 | (1) |
|
|
246 | (3) |
|
Chapter 10 Single-Molecule Cut and Paste |
|
|
249 | (12) |
|
|
|
|
10.1 Molecular Manipulation at the Nanometer Length Scale |
|
|
249 | (1) |
|
10.2 DNA as a Programmable Building Block |
|
|
250 | (1) |
|
10.3 Load-Driven Unfolding Geometries of DNA |
|
|
251 | (1) |
|
10.4 Hierarchical Force System |
|
|
252 | (1) |
|
10.5 Accuracy of the Single-Molecule Cut and Paste Process |
|
|
253 | (2) |
|
|
255 | (3) |
|
10.6.1 Controlled Deposition of Nanoscale Objects |
|
|
255 | (1) |
|
10.6.1.1 Nanoparticle Self-Assembly on a DNA-Scaffold Written by Single-Molecule Cut and Paste |
|
|
255 | (1) |
|
10.6.1.2 Protein-Based SMCP |
|
|
256 | (2) |
|
10.6.2 SMCP Patterns as Standard for the Optimization of Super-Resolution Microscopy Techniques |
|
|
258 | (1) |
|
|
258 | (1) |
|
|
259 | (1) |
|
|
259 | (2) |
Index |
|
261 | |