Evidence map›Paper›PMID 18625237›Full record

ArticleJournal of molecular biology2008

Quantifying the structural requirements of the folding transition state of protein A and other systems.

Michael C Baxa, Karl F Freed, Tobin R Sosnick

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.0field-weighted citation impact, top 26% of its field
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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Cooperative hydrophobic core interactions in the β-trefoil architecture.Protein science : a publication of the Protein Society · 2021
    Article
  3. Review
  4. Article
  5. Article
  6. Even with nonnative interactions, the updated folding transition states of the homologs Proteins G & L are extensive and similar.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Article
  9. Revealing what gets buried first in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Article
  11. Take home lessons from studies of related proteins.Current opinion in structural biology · 2013
    Review
  12. De novo prediction of protein folding pathways and structure using the principle of sequential stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Article
  14. Article
  15. Article
  16. The folding of single domain proteins--have we reached a consensus?Current opinion in structural biology · 2011
    Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Michael C BaxaDepartment of Physics, University of Chicago, 929 E. 57th St., Chicago, IL 60637, USA.
Karl F Freed
Tobin R Sosnick
University of Chicago · US

Funding

Kinetic studies of protein foldingR01GM055694 · NIGMS · UNIVERSITY OF CHICAGO · PI SOSNICK, TOBIN R · 2001 to 2022
$7.6M
Protein Structure Refinement Using a Novel MovesetR01GM081642 · NIGMS · UNIVERSITY OF CHICAGO · PI SOSNICK, TOBIN R · 2007 to 2009
$968k
NIGMS NIH HHS R01 GM055694NIGMS NIH HHS R01 GM081642
6 · The paper itself

Abstract

The B-domain of protein A is a small three-helix bundle that has been the subject of considerable experimental and theoretical investigation. Nevertheless, a unified view of the structure of the transition-state ensemble (TSE) is still lacking. To characterize the TSE of this surprisingly challenging protein, we apply a combination of psi analysis (which probes the role of specific side-chain to side-chain contacts) and kinetic H/D amide isotope effects (which measures hydrogen-bond content), building upon previous studies using mutational phi analysis (which probes the energetic influence of side-chain substitutions). The second helix is folded in the TSE, while helix formation appears just at the carboxy and amino termini of the first and third helices, respectively. The experimental data suggest a homogenous yet plastic TS with a native-like topology. This study generalizes our earlier conclusion, based on two larger alpha/beta proteins, that the TSEs of most small proteins achieve approximately 70% of their native state's relative contact order. This high percentage limits the degree of possible TS heterogeneity and requires a reevaluation of the structural content of the TSE of other proteins, especially when they are characterized as small or polarized.

Indexed as

Protein FoldingAmidesAmino Acid SequenceComputer SimulationGuanidineHydrogen BondingIsotopesKineticsModels, BiologicalModels, MolecularMolecular Sequence DataMutant ProteinsStaphylococcal Protein AThermodynamicsZincAmidesGuanidineIsotopesMutant ProteinsStaphylococcal Protein AZinc

Identifiers

PMID18625237
PMCPMC2742318
OpenAlexW1998966683

What OpenQuestion holds

Textmetadata
LicenceTDM
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.