Evidence map›Paper›PMID 20138892›Full record

ArticleJournal of molecular biology2010

A survey of lambda repressor fragments from two-state to downhill folding.

Feng Liu, Yi Gui Gao, Martin Gruebele

Abstract readComparative Study
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Fast pressure-jump all-atom simulations and experiments reveal site-specific protein dehydration-folding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  5. Article
  6. The Surface of Protein λBiochemistry · 2017
    Article
  7. How cooperative are protein folding and unfolding transitions?Protein science : a publication of the Protein Society · 2016
    Review
  8. Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchange.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Sequence, structure, and cooperativity in folding of elementary protein structural motifs.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Mapping fast protein folding with multiple-site fluorescent probes.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Fast protein folding kinetics.Quarterly reviews of biophysics · 2014
    Review
  12. Article
  13. Article
  14. Dodine as a protein denaturant: the best of two worlds?The journal of physical chemistry. B · 2013
    Article
  15. Misplaced helix slows down ultrafast pressure-jump protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. The fast and the slow: folding and trapping of λ6-85.Journal of the American Chemical Society · 2011
    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.

Feng LiuCenter for Biophysics and Computational Biology, University of Illinois, Urbana, IL 61801, USA.
Yi Gui Gao
Martin Gruebele

Funding

X-RAY STUDIES OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE BRAIN TISSUEP41RR008630 · NCRR · ILLINOIS INSTITUTE OF TECHNOLOGY · PI DE TOMBE, PIETER P. · 2001 to 2011
$14.4M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Protein refolding and transient aggregate formation studied by very fast pressureR01GM093318 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI GRUEBELE, MARTIN · 2010 to 2020
$3.1M
NCRR NIH HHS P41 RR008630NIBIB NIH HHS P30 EB009998NIGMS NIH HHS R01 GM093318
6 · The paper itself

Abstract

We survey the two-state to downhill folding transition by examining 20 lambda(6-85)* mutants that cover a wide range of stabilities and folding rates. We investigated four new lambda(6-85)* mutants designed to fold especially rapidly. Two were engineered using the core remodeling of Lim and Sauer, and two were engineered using Ferreiro et al.'s frustratometer. These proteins have probe-dependent melting temperatures as high as 80 degrees C and exhibit a fast molecular phase with the characteristic temperature dependence of the amplitude expected for downhill folding. The survey reveals a correlation between melting temperature and downhill folding previously observed for the beta-sheet protein WW domain. A simple model explains this correlation and predicts the melting temperature at which downhill folding becomes possible. An X-ray crystal structure with a 1.64-A resolution of a fast-folding mutant fragment shows regions of enhanced rigidity compared to the full wild-type protein.

Indexed as

Models, MolecularProtein FoldingBacteriophagesCrystallography, X-RayKineticsModels, ChemicalMutationProtein Structure, TertiaryRepressor ProteinsThermodynamicsViral Regulatory and Accessory Proteinsphage repressor proteinsRepressor ProteinsViral Regulatory and Accessory Proteins

Identifiers

PMID20138892
PMCPMC3740950

What OpenQuestion holds

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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.