Protein Structure, Stability, and Interactions
In the areas of biochemistry and cell biology, characterizations of stability and molecular interactions call for a quantitative approach with a level of precision that matches the fine tuning of these interactions in a living cell. Supporting and up-dating previous Methods in Molecular Biology™ vol...
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| Format: | eBook |
| Language: | English |
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Totowa, NJ
Humana
2009, 2009
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| Edition: | 1st ed. 2009 |
| Series: | Methods in Molecular Biology
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| Online Access: | |
| Collection: | Springer eBooks 2005- - Collection details see MPG.ReNa |
Table of Contents:
- Microcalorimetry of Proteins and Their Complexes
- Determining the Conformational Stability of a Protein Using Urea Denaturation Curves
- Defining the Stability of Multimeric Proteins
- Protein–Protein and Ligand–Protein Interactions Studied by Analytical Ultracentrifugation
- Monitoring Molecular Interactions by NMR
- Ligand-Binding Interactions and Stability
- A Method for Direct Measurement of Protein Stability In Vivo
- Quantifying the Roles of Water and Solutes (Denaturants, Osmolytes, and Hofmeister Salts) in Protein and Model Processes Using the Solute Partitioning Model
- Molecular Crowding and Solvation: Direct and Indirect Impact on Protein Reactions
- Defining the Role of Salt Bridges in Protein Stability
- Protein Stabilization by the Rational Design of Surface Charge–Charge Interactions
- NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange
- Single-Molecule Fluorescence Studies of Protein Folding
- Experimental Characterization of the Denatured State Ensemble of Proteins