ArticleBiophysical journal2009
Tensile mechanics of alanine-based helical polypeptide: force spectroscopy versus computer simulations.
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 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Correlation between chemical denaturation and the unfolding energetics of Acanthamoeba actophorin.Biophysical journal · 2023Article
- Accelerated Mechanochemistry in Helical Polymers.Angewandte Chemie (International ed. in English) · 2022Article
- Contribution of hydrophobic interactions to protein mechanical stability.Computational and structural biotechnology journal · 2022Article
- Nanoscale Molecular Characterization of Hair Cuticle Cells Using Integrated Atomic Force Microscopy-Infrared Laser Spectroscopy.Applied spectroscopy · 2020Article
- Do Skeletal Dynamics Mediate Sugar Uptake and Transport in Human Erythrocytes?Biophysical journal · 2018Article
- Molecular basis of the mechanical hierarchy in myomesin dimers for sarcomere integrity.Biophysical journal · 2014Article
- Two-phase stretching of molecular chains.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A rigidity-enhanced antimicrobial activity: a case for linear cationic α-helical peptide HP(2-20) and its four analogues.PloS one · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In nature, an alpha-helix is commonly used to build thermodynamically stable and mechanically rigid protein conformations. In view of growing interest in the mechanical rigidity of proteins, we measured the tensile profile of an alanine-based alpha-helical polypeptide on an atomic-force microscope to investigate the basic mechanics of helix extension with minimal interference from side-chain interactions. The peptide was extended to its maximum contour length with much less force than in reported cases of poly-L-Glu or poly-L-Lys, indicating that chain stiffness strongly depended on the physicochemical properties of side chains, such as their bulkiness. The low tensile-force extension originated presumably in locally unfolded parts because of spontaneous structural fluctuations. In 50% trifluoroethanol, the well-known helix-promoting agent, the rigidity of the sample polypeptide was markedly increased. Computer simulations of the peptide-stretching process showed that a majority of constituent residues underwent a transition from an alpha-helical to an extended conformation by overcoming an energy barrier around psi approximately 0 degrees on the Ramachandran plot. The observed lability of an isolated helix signified the biological importance of the lateral bundling of helices to maintain a rigid protein structure.
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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.