التفاصيل البيبلوغرافية
العنوان: |
Measuring membrane protein stability under native conditions |
المؤلفون: |
Chang, Yu-Chu, Bowie, James U |
المصدر: |
Proceedings of the National Academy of Sciences of the United States of America, vol 111, iss 1 |
بيانات النشر: |
eScholarship, University of California |
سنة النشر: |
2014 |
المجموعة: |
University of California: eScholarship |
مصطلحات موضوعية: |
Bacteriorhodopsins, Biotin, Biotinylation, Dimyristoylphosphatidylcholine, Halobacterium salinarum, Kinetics, Lipid Bilayers, Membrane Proteins, Micelles, Protein Denaturation, Protein Folding, Protein Stability, Protein Structure, Secondary, Temperature, Thermodynamics, membrane protein folding, steric trap |
جغرافية الموضوع: |
219 - 224 |
الوصف: |
The thermodynamic stability of proteins is typically measured at high denaturant concentrations and then extrapolated back to zero denaturant conditions to obtain unfolding free energies under native conditions. For membrane proteins, the extrapolations are fraught with considerable uncertainty as the denaturants may have complex effects on the membrane or micellar structure. We therefore sought to measure stability under native conditions, using a method that does not perturb the properties of the membrane or membrane mimetics. We use a technique called steric trapping to measure the thermodynamic stability of bacteriorhodopsin in bicelles and micelles. We find that bacteriorhodopsin has a high thermodynamic stability, with an unfolding free energy of ∼11 kcal/mol in dimyristoyl phosphatidylcholine bicelles. Nevertheless, the stability is much lower than predicted by extrapolation of measurements made at high denaturant concentrations. We investigated the discrepancy and found that unfolding free energy is not linear with denaturant concentration. Apparently, long extrapolations of helical membrane protein unfolding free energies must be treated with caution. Steric trapping, however, provides a method for making these measurements. |
نوع الوثيقة: |
article in journal/newspaper |
وصف الملف: |
application/pdf |
اللغة: |
unknown |
العلاقة: |
qt9hh223z9; https://escholarship.org/uc/item/9hh223z9Test |
الإتاحة: |
https://escholarship.org/uc/item/9hh223z9Test |
حقوق: |
public |
رقم الانضمام: |
edsbas.C9B13871 |
قاعدة البيانات: |
BASE |