ArticleProceedings of the National Academy of Sciences of the United States of America2000
Native topology determines force-induced unfolding pathways in globular proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
63 citing papers in PubMed.
- Computational design of superstable proteins through maximized hydrogen bonding.Nature chemistry · 2026Article
- Asymmetry in histone rotation in forced unwrapping and force quench rewrapping in a nucleosome.Nucleic acids research · 2021Article
- Entropic bonding of the type 1 pilus from experiment and simulation.Royal Society open science · 2020Article
- Protein unfolding by SDS: the microscopic mechanisms and the properties of the SDS-protein assembly.Nanoscale · 2020Article
- FcαRI binding at the IgA1 CProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Forced-rupture of cell-adhesion complexes reveals abrupt switch between two brittle states.The Journal of chemical physics · 2018Article
- Mechanical Deformation Mechanisms and Properties of Prion Fibrils Probed by Atomistic Simulations.Nanoscale research letters · 2017Article
- Reduction of All-Atom Protein Folding Dynamics to One-Dimensional Diffusion.The journal of physical chemistry. B · 2015Article
- Dependence of internal friction on folding mechanism.Journal of the American Chemical Society · 2015Article
- Force-induced remodelling of proteins and their complexes.Current opinion in structural biology · 2015Review
- Functional Importance of Mobile Ribosomal Proteins.BioMed research international · 2015Review
- Connecting thermal and mechanical protein (un)folding landscapes.Biophysical journal · 2014Article
- Sequence-dependent folding landscapes of adenine riboswitch aptamers.Physical chemistry chemical physics : PCCP · 2014Article
- COARSE-GRAINED MODELING OF PROTEIN UNFOLDING DYNAMICS.Multiscale modeling & simulation : a SIAM interdisciplinary journal · 2014Article
- Reconstructing folding energy landscapes by single-molecule force spectroscopy.Annual review of biophysics · 2014Review
- Mechanical resistance in unstructured proteins.Biophysical journal · 2013Article
- Exact solution of the Zwanzig-Lauritzen model of polymer crystallization under tension.The Journal of chemical physics · 2013Article
- The molecular mechanism underlying mechanical anisotropy of the protein GB1.Biophysical journal · 2012Article
- Denaturant-dependent folding of GFP.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Single-molecule experiments reveal the flexibility of a Per-ARNT-Sim domain and the kinetic partitioning in the unfolding pathway under force.Biophysical journal · 2012Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-molecule manipulation techniques reveal that stretching unravels individually folded domains in the muscle protein titin and the extracellular matrix protein tenascin. These elastic proteins contain tandem repeats of folded domains with beta-sandwich architecture. Herein, we propose by stretching two model sequences (S1 and S2) with four-stranded beta-barrel topology that unfolding forces and pathways in folded domains can be predicted by using only the structure of the native state. Thermal refolding of S1 and S2 in the absence of force proceeds in an all-or-none fashion. In contrast, phase diagrams in the force-temperature (f,T) plane and steered Langevin dynamics studies of these sequences, which differ in the native registry of the strands, show that S1 unfolds in an allor-none fashion, whereas unfolding of S2 occurs via an obligatory intermediate. Force-induced unfolding is determined by the native topology. After proving that the simulation results for S1 and S2 can be calculated by using native topology alone, we predict the order of unfolding events in Ig domain (Ig27) and two fibronectin III type domains ((9)FnIII and (10)FnIII). The calculated unfolding pathways for these proteins, the location of the transition states, and the pulling speed dependence of the unfolding forces reflect the differences in the way the strands are arranged in the native states. We also predict the mechanisms of force-induced unfolding of the coiled-coil spectrin (a three-helix bundle protein) for all 20 structures deposited in the Protein Data Bank. Our approach suggests a natural way to measure the phase diagram in the (f,C) plane, where C is the concentration of denaturants.
Indexed as
Identifiers
What OpenQuestion holds
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.