𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Intermolecular forces in the process of heat aggregation of globular proteins and the problem of correlation between aggregation and denaturation phenomena

✍ Scribed by Jaenicke, R.


Publisher
Wiley (John Wiley & Sons)
Year
2007
Weight
961 KB
Volume
16
Category
Article
ISSN
0449-2994

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Insight into the correlation between lag
✍ Stefan Auer; Dimo Kashchiev πŸ“‚ Article πŸ“… 2010 πŸ› John Wiley and Sons 🌐 English βš– 407 KB

## Abstract Under favorable conditions, many proteins can assemble into macroscopically large aggregates such as the amyloid fibrils that are associated with Alzheimer's, Parkinson's, and other neurological and systemic diseases. The overall process of protein aggregation is characterized by initia

II. Electrostatic effect in the aggregat
✍ Amos M. Tsai; John H. van Zanten; Michael J. Betenbaugh πŸ“‚ Article πŸ“… 1998 πŸ› John Wiley and Sons 🌐 English βš– 79 KB πŸ‘ 2 views

In the previous study (part I), heat-denatured RNase A aggregation was shown to depend on the solution pH. Interestingly, at pH 3.0, the protein did not aggregate even when exposed to 75Β°C for 24 h. In this study, electrostatic repulsion was shown to be responsible for the absence of aggregates at t

Reversibility of thermal transitions in
✍ B. S. Harrap πŸ“‚ Article πŸ“… 1969 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 749 KB

The reversibility of the thermal denaturation of a low-sulfur fraction of solubilized wool keratin (SCMKA) has been studied under a variety of conditions of time, protein concentration, and pH. Two types of irreversibility for the transition have been encountered. One of these is associated with an