ArticleBiophysical journal2009
Combining single-molecule optical trapping and small-angle x-ray scattering measurements to compute the persistence length of a protein ER/K alpha-helix.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 44 citations in OpenAlex.
- Anomalous photophysical behaviors attributed to excitonic coupling in fluorescent proteins.Biophysical journal · 2025Article
- Optical trapping and manipulating with a transmissive and polarization-insensitive metalens.Nanophotonics (Berlin, Germany) · 2024Article
- Tad and toxin-coregulated pilus structures reveal unexpected diversity in bacterial type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Engineering the Active Site Lid Dynamics to Improve the Catalytic Efficiency of Yeast Cytosine Deaminase.International journal of molecular sciences · 2023Article
- Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022Article
- Förster resonance energy transfer biosensors for fluorescence and time-gated luminescence analysis of rac1 activity.Scientific reports · 2022Article
- ER/K-link-Leveraging a native protein linker to probe dynamic cellular interactions.Methods in enzymology · 2021Review
- Modulating the Stiffness of the Myosin VI Single α-Helical Domain.Biophysical journal · 2020Article
- Remarkable Rigidity of the Single α-Helical Domain of Myosin-VI As Revealed by NMR Spectroscopy.Journal of the American Chemical Society · 2019Article
- ER/K linked GPCR-G protein fusions systematically modulate second messenger response in cells.Scientific reports · 2017Article
- Protein Interaction Analysis Provides a Map of the Spatial and Temporal Organization of the Ciliary Gating Zone.Current biology : CB · 2017Article
- Characterization of long and stable de novo single alpha-helix domains provides novel insight into their stability.Scientific reports · 2017Article
- Carbonyl reductase identification and development of whole-cell biotransformation for highly efficient synthesis of (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol.Microbial cell factories · 2016Article
- Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.Biophysical journal · 2016Article
- Using Kinetic Network Models To Probe Non-Native Salt-Bridge Effects on α-Helix Folding.The journal of physical chemistry. B · 2016Article
- A method for multiprotein assembly in cells reveals independent action of kinesins in complex.The Journal of cell biology · 2014Article
- Stable single α-helices are constant force springs in proteins.The Journal of biological chemistry · 2014Article
- Harnessing the unique structural properties of isolated α-helices.The Journal of biological chemistry · 2014Article
- Myosin VI must dimerize and deploy its unusual lever arm in order to perform its cellular roles.Cell reports · 2014Article
- Conserved modular domains team up to latch-open active protein kinase Cα.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
A relatively unknown protein structure motif forms stable isolated single alpha-helices, termed ER/K alpha-helices, in a wide variety of proteins and has been shown to be essential for the function of some molecular motors. The flexibility of the ER/K alpha-helix determines whether it behaves as a force transducer, rigid spacer, or flexible linker in proteins. In this study, we quantify this flexibility in terms of persistence length, namely the length scale over which it is rigid. We use single-molecule optical trapping and small-angle x-ray scattering, combined with Monte Carlo simulations to demonstrate that the Kelch ER/K alpha-helix behaves as a wormlike chain with a persistence length of approximately 15 nm or approximately 28 turns of alpha-helix. The ER/K alpha-helix length in proteins varies from 3 to 60 nm, with a median length of approximately 5 nm. Knowledge of its persistence length enables us to define its function as a rigid spacer in a translation initiation factor, as a force transducer in the mechanoenzyme myosin VI, and as a flexible spacer in the Kelch-motif-containing protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.