ArticleBiophysical journal2012
A delicate interplay of structure, dynamics, and thermodynamics for function: a high pressure NMR study of outer surface protein A.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 30 citations in OpenAlex.
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Design of a broadly reactive Lyme disease vaccine.NPJ vaccines · 2020Article
- How internal cavities destabilize a protein.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Water-Protein Interactions Coupled with Protein Conformational Transition.Biophysical journal · 2018Article
- Analysis of OBiophysical journal · 2017Article
- Amide hydrogens reveal a temperature-dependent structural transition that enhances site-II CaScientific reports · 2017Article
- Structural basis for the dissociation of α-synuclein fibrils triggered by pressure perturbation of the hydrophobic core.Scientific reports · 2016Article
- Tick receptor for outer surface protein A from Ixodes ricinus - the first intrinsically disordered protein involved in vector-microbe recognition.Scientific reports · 2016Article
- Detecting O2 binding sites in protein cavities.Scientific reports · 2016Article
- Cavity as a source of conformational fluctuation and high-energy state: high-pressure NMR study of a cavity-enlarged mutant of T4 lysozyme.Biophysical journal · 2015Article
- Transient conformational fluctuation of TePixD during a reaction.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Volume of Hsp90 ligand binding and the unfolding phase diagram as a function of pressure and temperature.European biophysics journal : EBJ · 2013Article
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Authors and funding
7 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Outer surface protein A (OspA) is a crucial protein in the infection of Borrelia burgdorferi causing Lyme disease. We studied conformational fluctuations of OspA with high-pressure (15)N/(1)H two-dimensional NMR along with high-pressure fluorescence spectroscopy. We found evidence within folded, native OspA for rapid local fluctuations of the polypeptide backbone in the nonglobular single layer β-sheet connecting the N- and C-terminal domains with τ << ms, which may give the two domains certain independence in mobility and thermodynamic stability. Furthermore, we found that folded, native OspA is in equilibrium (τ >> ms) with a minor conformer I, which is almost fully disordered and hydrated for the entire C-terminal part of the polypeptide chain from β8 to the C-terminus. Conformer I is characterized with ΔG(0) = 32 ± 9 kJ/mol and ΔV(0) = -140 ± 40 mL/mol, populating only ∼0.001% at 40°C at 0.1 MPa, pH 5.9. Because in the folded conformer the receptor binding epitope of OspA is buried in the C-terminal domain, its transition into conformer I under in vivo conditions may be critical for the infection of B. burgdorferi. The formation and stability of the peculiar conformer I are apparently supported by a large packing defect or cavity located in the C-terminal domain.
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