ArticleNano letters2008
Factors governing helix formation in peptides confined to carbon nanotubes.
Article in Nano letters, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Effects of Molecular Crowding on the Structural, Dynamic, and Functional Properties of Biological Macromolecules: A General Overview.Sub-cellular biochemistry · 2025Review
- (Macro)Molecular Crowding Effects Beyond Volume Exclusion.Sub-cellular biochemistry · 2025Review
- Ribosome Tunnel Environment Drives the Formation of α-Helix during Cotranslational Folding.Journal of chemical information and modeling · 2024Article
- How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024Review
- How Nanopore Translocation Experiments Can Measure RNA Unfolding.Biophysical journal · 2020Article
- Dynamics of Co-translational Membrane Protein Integration and Translocation via the Sec Translocon.Journal of the American Chemical Society · 2020Review
- Beyond the excluded volume effects: mechanistic complexity of the crowded milieu.Molecules (Basel, Switzerland) · 2015Review
- Probing hemoglobin confinement inside submicron silica tubes using synchrotron SAXS and electrochemical response.European biophysics journal : EBJ · 2013Article
- Kinetic analysis of ribosome-bound fluorescent proteins reveals an early, stable, cotranslational folding intermediate.The Journal of biological chemistry · 2012Article
- Energy landscape of the prion protein helix 1 probed by metadynamics and NMR.Biophysical journal · 2012Article
- Binding of blood proteins to carbon nanotubes reduces cytotoxicity.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Free energy of nascent-chain folding in the translocon.Journal of the American Chemical Society · 2011Article
- Assisted peptide folding by surface pattern recognition.Biophysical journal · 2011Article
- Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition.Biophysical journal · 2009Article
- An alpha-helical peptide in AOT micelles prefers to be localized at the water/headgroup interface.Biophysical journal · 2009Article
- Water-mediated interactions between hydrophobic and ionic species in cylindrical nanopores.The Journal of chemical physics · 2009Article
- Interactions between amino acid side chains in cylindrical hydrophobic nanopores with applications to peptide stability.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
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Authors and funding
4 authors.
Funding
Abstract
The effect of confinement on the stability and dynamics of peptides and proteins is relevant in the context of a number of problems in biology and biotechnology. We have examined the stability of different helix-forming sequences upon confinement to a carbon nanotube using Langevin dynamics simulations of a coarse-grained representation of the polypeptide chain. We show that the interplay of several factors that include sequence, solvent conditions, strength (lambda) of nanotube-peptide interactions, and the nanotube diameter (D) determines confinement-induced stability of helicies. In agreement with predictions based on polymer theory, the helical state is entropically stabilized for all sequences when the interaction between the peptide and the nanotube is weakly hydrophobic and D is small. However, there is a strong sequence dependence as the strength of the lambda increases. For an amphiphilic sequence, the helical stability increases with lambda, whereas for polyalanine the diagram of states is a complex function of lambda and D. In addition, decreasing the size of the "hydrophobic patch" lining the nanotube, which mimics the chemical heterogeneity of the ribosome tunnel, increases the helical stability of the polyalanine sequence. Our results provide a framework for interpreting a number of experiments involving the structure formation of peptides in the ribosome tunnel as well as transport of biopolymers through nanotubes.
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