Evidence map›Paper›PMID 18093935›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

Axis-dependent anisotropy in protein unfolding from integrated nonequilibrium single-molecule experiments, analysis, and simulation.

Rene A Nome, Jason Ming Zhao, Wouter D Hoff, Norbert F Scherer

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. BSDB: the biomolecule stretching database.Nucleic acids research · 2011
    Article
  9. Free energy profiles from single-molecule pulling experiments.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Rene A NomeDepartment of Chemistry, Institute for Biophysical Dynamics, 929 East 57th Street, University of Chicago, Chicago, IL 60637, USA.
Jason Ming Zhao
Wouter D Hoff
Norbert F Scherer

Funding

Predoctoral Training Program in Chemistry & BiologyT32GM008720 · NIGMS · UNIVERSITY OF CHICAGO · PI PICCIRILLI, JOSEPH ANTHONY · 1999 to 2020
$4.7M
Partial Protein Unfolding as a Novel Signaling MechanismR01GM063805 · NIGMS · UNIVERSITY OF CHICAGO · PI HOFF, WOUTER D · 2001 to 2005
$1.1M
NIGMS NIH HHS GM008720NIGMS NIH HHS GM63805NIGMS NIH HHS R01 GM063805NIGMS NIH HHS T32 GM008720
6 · The paper itself

Abstract

We present a comprehensive study that integrates experimental and theoretical nonequilibrium techniques to map energy landscapes along well defined pull-axis specific coordinates to elucidate mechanisms of protein unfolding. Single-molecule force-extension experiments along two different axes of photoactive yellow protein combined with nonequilibrium statistical mechanical analysis and atomistic simulation reveal energetic and mechanistic anisotropy. Steered molecular dynamics simulations and free-energy curves constructed from the experimental results reveal that unfolding along one axis exhibits a transition-state-like feature where six hydrogen bonds break simultaneously with weak interactions observed during further unfolding. The other axis exhibits a constant (unpeaked) force profile indicative of a noncooperative transition, with enthalpic (e.g., H-bond) interactions being broken throughout the unfolding process. Striking qualitative agreement was found between the force-extension curves derived from steered molecular dynamics calculations and the equilibrium free-energy curves obtained by Jarzynski-Hummer-Szabo analysis of the nonequilibrium work data. The anisotropy persists beyond pulling distances of more than twice the initial dimensions of the folded protein, indicating a rich energy landscape to the mechanically fully unfolded state. Our findings challenge the notion that cooperative unfolding is a universal feature in protein stability.

Indexed as

AnisotropyProtein ConformationProtein DenaturationBacterial ProteinsBiophysicsComputer SimulationCysteineHalorhodospira halophilaHydrogen BondingKineticsLuminescent ProteinsMicroscopy, Atomic ForceMolecular ConformationProtein BindingProtein FoldingProtein Structure, SecondaryBacterial ProteinsCysteineLuminescent Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID18093935
PMCPMC2410074

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.