| 1.1 |
 |
Introduction |
| 1.2 |
Materials |
| 1.3 |
Methods |
| 1.3.1 |
Physical adsorption of proteins on carbon nanotubes |
| 1.3.2 |
Protein assisted solubilization of carbon nanotubes |
| 1.3.3 |
Covalent attachment of proteins onto carbon nanotubes |
| 1.4 |
Data acquisition, anticipated results, and interpretation of data |
| 1.4.1 |
Characterization of proteins physically adsorbed onto carbon nanotubes |
| 1.4.1.1 |
Measurement of loading of proteins on carbon nanotubes by the BCA assay |
| 1.4.1.2 |
Retention of protein activity upon physical adsorption |
| 1.4.1.2.1 |
Determination of protein activity upon physical adsorption |
| 1.4.1.2.2 |
Protein stability under harsh conditions |
| 1.4.1.3 |
Determination of protein secondary structure using Fourier Transform Infrared (FT-IR) Spectroscopy |
| 1.4.2 |
Characterization of protein-solubilized carbon nanotubes |
| 1.4.2.1 |
Characterization of carbon nanotube dispersions using UV-Vis Spectroscopy |
| 1.4.2.2 |
Raman spectroscopy to probe aggregation state of SWNTs |
| 1.4.3 |
Characterization of covalently attached carbon nanotube-protein conjugates |
| 1.4.3.1 |
Hammett Analysis for protein structure-activity relationship |
| 1.4.3.2 |
Determination of Protein Secondary Structure using Circular Dichroism (CD) Spectroscopy |
| 1.4.3.3 |
Characterization of Protein Tertiary Structure using Tryptophan Fluorescence |
| 1.4.3.4 |
Thermostabilization of proteins via covalent attachment onto carbon nanotubes |
| 1.4.3.5 |
Operational and storage stability of carbon nanotube-enzyme conjugates |
| 1.5 |
Discussion and Commentary |
| 1.6 |
Troubleshooting Table |
| 1.7 |
Application Notes |
| 1.8 |
Summary points: |
| 1.9 |
Acknowledgements: |
| 1.10 |
References |
