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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sharpe, Timothy D. Neuweiler, Hannes Johnson, Christopher M. Fersht, Alan R. Arbely, Eyal |
| Description | Country affiliation: United kingdom Author Affiliation: Arbely E ( Medical Research Council Centre for Protein Engineering, Cambridge, United Kingdom.) |
| Abstract | Peripheral subunit binding domains (PSBDs) are integral parts of large multienzyme complexes involved in carbohydrate metabolism. PSBDs facilitate shuttling of prosthetic groups between different catalytic subunits. Their protein surface is characterized by a high density of positive charges required for binding to subunits within the complex. Here, we investigated folding thermodynamics and kinetics of the human PSBD (HSBD) using circular dichroism and tryptophan fluorescence experiments. HSBD was only marginally stable under physiological solvent conditions but folded within microseconds via a barrier-limited apparent two-state transition, analogous to its bacterial homologues. The high positive surface-charge density of HSBD leads to repulsive Coulomb forces that modulate protein stability and folding kinetics, and appear to even induce native-state movement. The electrostatic strain was alleviated at high solution-ionic-strength by Debye-Hückel screening. Differences in ionic-strength dependent characteristics among PSBD homologues could be explained by differences in their surface charge distributions. The findings highlight the trade-off between protein function and stability during protein evolution. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| DOI | 10.1002/pro.453 |
| Journal | Protein Science |
| Issue Number | 9 |
| Volume Number | 19 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 2010-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Pyruvate Dehydrogenase Complex Chemistry Amino Acid Sequence Circular Dichroism Models, Molecular Molecular Sequence Data Osmolar Concentration Protein Denaturation Protein Folding Protein Stability Sequence Alignment Spectrometry, Fluorescence Structural Homology, Protein Thermodynamics Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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