Slow unfolding explains high stability of thermostable ferredoxins: common mechanism governing thermostability?
✍ Scribed by Pernilla Wittung-Stafshede
- Book ID
- 104003307
- Publisher
- Elsevier Science
- Year
- 2004
- Tongue
- English
- Weight
- 138 KB
- Volume
- 1700
- Category
- Article
- ISSN
- 1570-9639
No coin nor oath required. For personal study only.
✦ Synopsis
The role of kinetics in governing exceptional stability of thermophilic ferredoxins has been explored. Strikingly, unfolding-rate constants (pH 7, 20 jC) are over eight (log 10 ) orders of magnitude slower for the thermophiles than for a large set of unrelated mesophilic proteins. Also at low pH, where ionic interactions are diminished, unfolding of the thermophilic ferredoxins is significantly slower than unfolding of the mesophiles at pH 7, emphasizing the importance of hydrophobic interactions. A kinetic barrier towards unfolding may be a common strategy used by many proteins to withstand extreme conditions.