ArticleNature nanotechnology2009
Determination of protein structural flexibility by microsecond force spectroscopy.
Article in Nature nanotechnology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Elastic analysis bridges structure and dynamics of an AAA+ molecular motor.PLoS computational biology · 2025Article
- Understanding the Rhodopsin Worldview Through Atomic Force Microscopy (AFM): Structure, Stability, and Activity Studies.Chemical record (New York, N.Y.) · 2023Review
- Detecting Individual Proteins and Their Surface Charge Variations in Solution by the Potentiometric Nanoimpact Method.ACS sensors · 2022Article
- Conformational Transitions of Amyloid-β: A Langevin and Generalized Langevin Dynamics Simulation Study.ACS omega · 2021Article
- Calibration of T-shaped atomic force microscope cantilevers using the thermal noise method.The Review of scientific instruments · 2020Article
- Cellular nanoscale stiffness patterns governed by intracellular forces.Nature materials · 2019Article
- Differentiating between Inactive and Active States of Rhodopsin by Atomic Force Microscopy in Native Membranes.Analytical chemistry · 2019Article
- Fast and high-resolution mapping of elastic properties of biomolecules and polymers with bimodal AFM.Nature protocols · 2018Article
- Properties of Omp2a-Based Supported Lipid Bilayers: Comparison with Polymeric Bioinspired Membranes.ACS omega · 2018Article
- X-ray diffraction reveals the intrinsic difference in the physical properties of membrane and soluble proteins.Scientific reports · 2017Article
- Imaging modes of atomic force microscopy for application in molecular and cell biology.Nature nanotechnology · 2017Review
- Scaling law to determine peak forces in tapping-mode AFM experiments on finite elastic soft matter systems.Beilstein journal of nanotechnology · 2017Article
- A Structure-free Method for Quantifying Conformational Flexibility in proteins.Scientific reports · 2016Article
- Identification of a Novel Parallel β-Strand Conformation within Molecular Monolayer of Amyloid Peptide.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2016Article
- Imaging and three-dimensional reconstruction of chemical groups inside a protein complex using atomic force microscopy.Nature nanotechnology · 2015Article
- High-speed AFM images of thermal motion provide stiffness map of interfacial membrane protein moieties.Nano letters · 2015Article
- Hierarchical Conformational Analysis of Native Lysozyme Based on Sub-Millisecond Molecular Dynamics Simulations.PloS one · 2015Article
- Mapping of elasticity and damping in an α + β titanium alloy through atomic force acoustic microscopy.Beilstein journal of nanotechnology · 2015Article
- Multiparametric high-resolution imaging of native proteins by force-distance curve-based AFM.Nature protocols · 2014Article
- Mg2+ effect on argonaute and RNA duplex by molecular dynamics and bioinformatics implications.PloS one · 2014Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins are dynamic molecular machines having structural flexibility that allows conformational changes. Current methods for the determination of protein flexibility rely mainly on the measurement of thermal fluctuations and disorder in protein conformations and tend to be experimentally challenging. Moreover, they reflect atomic fluctuations on picosecond timescales, whereas the large conformational changes in proteins typically happen on micro- to millisecond timescales. Here, we directly determine the flexibility of bacteriorhodopsin -- a protein that uses the energy in light to move protons across cell membranes -- at the microsecond timescale by monitoring force-induced deformations across the protein structure with a technique based on atomic force microscopy. In contrast to existing methods, the deformations we measure involve a collective response of protein residues and operate under physiologically relevant conditions with native proteins.
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