Evidence map›Paper›PMID 22109973›Full record

ReviewProtein science : a publication of the Protein Society2012

Spectroscopic studies of protein folding: linear and nonlinear methods.

Arnaldo L Serrano, Matthias M Waegele, Feng Gai

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed.

  1. Article
  2. Review
  3. A TeZla micromixer for interrogating the early and broad folding landscape of G-quadruplex via multistage velocity descending.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Coordination to lanthanide ions distorts binding site conformation in calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Dual time-resolved temperature-jump fluorescence and infrared spectroscopy for the study of fast protein dynamics.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2017
    Article
  15. Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017
    Article
  16. Simple method to introduce an ester infrared probe into proteins.Protein science : a publication of the Protein Society · 2017
    Article
  17. Article
  18. Review
  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.

Arnaldo L SerranoDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
Matthias M Waegele
Feng Gai

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Spectroscopic Study of Protein Folding DynamicsR01GM065978 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2002 to 2014
$3.9M
NCRR NIH HHS RR01348NIGMS NIH HHS GM-065978NIGMS NIH HHS R01 GM065978
6 · The paper itself

Abstract

Although protein folding is a simple outcome of the underlying thermodynamics, arriving at a quantitative and predictive understanding of how proteins fold nevertheless poses huge challenges. Therefore, both advanced experimental and computational methods are continuously being developed and refined to probe and reveal the atomistic details of protein folding dynamics and mechanisms. Herein, we provide a concise review of recent developments in spectroscopic studies of protein folding, with a focus on new triggering and probing methods. In particular, we describe several laser-based techniques for triggering protein folding/unfolding on the picosecond and/or nanosecond timescales and various linear and nonlinear spectroscopic techniques for interrogating protein conformations, conformational transitions, and dynamics.

Indexed as

Protein FoldingAnimalsAzo CompoundsHumansKineticsLasersLinear ModelsModels, MolecularMolecular ConformationNonlinear DynamicsProteinsSpectrum AnalysisThermodynamicsazobenzeneAzo CompoundsProteins

Identifiers

PMID22109973
PMCPMC3324760

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.