Protein Stiffening and Entropic Stabilization in the Subdenaturing Limit of Guanidine Hydrochloride
β Scribed by Kumar, Rajesh; Prabhu, N. Prakash; Yadaiah, M.; Bhuyan, Abani K.
- Book ID
- 119918778
- Publisher
- Biophysical Society
- Year
- 2004
- Tongue
- English
- Weight
- 184 KB
- Volume
- 87
- Category
- Article
- ISSN
- 0006-3495
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
higher temperatures. The data presented here might be used to understand better, through the application of different models, the exposure of non-polar amino acid side chains from the protein interior to the aqueous environment, which characterizes protein denaturation.
A technique has been perfected for measuring the sedimentation coefficient of microgram quantities of a reduced protein in 6 M guanidine hydrochloride. The protein is sedimented through a gradient of 5-8 M guanidine-HCl in the presence of dithiothreitol in a SW 50.1 swinging-bucket rotor. Run condit