Evidence map›Paper›PMID 24372101›Full record

ArticleJournal of the American Chemical Society2014

Two-dimensional sum-frequency generation reveals structure and dynamics of a surface-bound peptide.

Jennifer E Laaser, David R Skoff, Jia-Jung Ho, Yongho Joo, Arnaldo L Serrano, Jay D Steinkruger, Padma Gopalan, Samuel H Gellman, Martin T Zanni

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Two-dimensional infrared spectroscopy measures the structural dynamics of a self-assembled film only one molecule thick.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Review
  10. Article
  11. Article
  12. Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015
    Article
  13. 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

9 authors.

Jennifer E LaaserDepartment of Chemistry and ‡Department of Materials Science and Engineering, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.
David R Skoff
Jia-Jung Ho
Yongho Joo
Arnaldo L Serrano
Jay D Steinkruger
Padma Gopalan
Samuel H Gellman
Martin T Zanni

Funding

Use of designed peptides to study folding and bindingR01GM061238 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GELLMAN, SAMUEL H. · 2000 to 2023
$7.9M
Structural mechanism of diabetic amyloid formationR01DK079895 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI Martin T Zanni · 2008 to 2026
$7.7M
PREDOCTORAL TRAINING IN MOLECULAR BIOPHYSICST32GM008293 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI JACKSON, MEYER B. · 1989 to 2016
$4.6M
NIDDK NIH HHS DK079895NIDDK NIH HHS R01 DK079895NIGMS NIH HHS R01 GM061238NIGMS NIH HHS T32 GM008293NIGMS NIH HHS T32-GM08293
6 · The paper itself

Abstract

Surface-bound polypeptides and proteins are increasingly used to functionalize inorganic interfaces such as electrodes, but their structural characterization is exceedingly difficult with standard technologies. In this paper, we report the first two-dimensional sum-frequency generation (2D SFG) spectra of a peptide monolayer, which are collected by adding a mid-IR pulse shaper to a standard femtosecond SFG spectrometer. On a gold surface, standard FTIR spectroscopy is inconclusive about the peptide structure because of solvation-induced frequency shifts, but the 2D line shapes, anharmonic shifts, and lifetimes obtained from 2D SFG reveal that the peptide is largely α-helical and upright. Random coil residues are also observed, which do not themselves appear in SFG spectra due to their isotropic structural distribution, but which still absorb infrared light and so can be detected by cross-peaks in 2D SFG spectra. We discuss these results in the context of peptide design. Because of the similar way in which the spectra are collected, these 2D SFG spectra can be directly compared to 2D IR spectra, thereby enabling structural interpretations of surface-bound peptides and biomolecules based on the well-studied structure/2D IR spectra relationships established from soluble proteins.

Indexed as

Amino Acid SequenceGoldModels, MolecularMolecular Sequence DataPeptidesProtein Structure, SecondarySpectrophotometry, InfraredSurface PropertiesGoldPeptides

Identifiers

PMID24372101
PMCPMC3956615

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.