ArticleScience advances2024
Probing the energy barriers and stages of membrane protein unfolding using solid-state NMR spectroscopy.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Atomic structure and dynamics of the mechanosensitive channel MscL fromScience advances · 2026Article
- Conformation-Determined Segmental Dynamics in α-Poly-l-Lysine Hydrobromide: The Impact of Thermally Induced β-Sheet Formation on the Glass Transition Temperature.The journal of physical chemistry. B · 2026Article
- A random fractionalMagnetic resonance letters · 2026Article
- A conserved H-bond network in human aquaporin-1 is necessary for native folding and oligomerization.Biophysical journal · 2024Article
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Authors and funding
5 authors.
Funding
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Abstract
Understanding how the amino acid sequence dictates protein structure and defines its stability is a fundamental problem in molecular biology. It is especially challenging for membrane proteins that reside in the complex environment of a lipid bilayer. Here, we obtain an atomic-level picture of the thermally induced unfolding of a membrane-embedded α-helical protein, human aquaporin 1, using solid-state nuclear magnetic resonance spectroscopy. Our data reveal the hierarchical two-step pathway that begins with unfolding of a structured extracellular loop and proceeds to an intermediate state with a native-like helical packing. In the second step, the transmembrane domain unravels as a single unit, resulting in a heterogeneous misfolded state with high helical content but with nonnative helical packing. Our results show the importance of loops for the kinetic stabilization of the whole membrane protein structure and support the three-stage membrane protein folding model.
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