Analysis of the conformational transitions of proteins by temperature-gradient gel electrophoresis
✍ Scribed by Andreas Birmes; Andrea Sättler; Karl-Heinz Maurer; Prof. Dr. Detlev Riesner
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 861 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0173-0835
No coin nor oath required. For personal study only.
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A new technique, temperature gradient gel electrophoresis (TGGE), was applied to the study of heat-induced protein denaturation. The gels used contained 30 mм Borax \(+75 \mathrm{~mm}\) boric acid, \(\mathrm{pH}\) 8.4, and various concentrations of urea. When this technique was applied to bovine ser
## Abstract The thermal unfolding of microbial serine proteases was studied by temperature‐gradient gel electrophoresis (TGGE). Conditions for a native polyacrylamide gel electrophoresis were established, and the temperature gradient was applied perpendicularly to the direction of electrophoretic m