Evidence map›Paper›PMID 23727992›Full record

ArticlePhysical chemistry chemical physics : PCCP2013

SFG analysis of surface bound proteins: a route towards structure determination.

Tobias Weidner, David G Castner

Abstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  6. Studies of Dynamic Binding of Amino Acids to TiOLangmuir : the ACS journal of surfaces and colloids · 2020
    Article
  7. Review
  8. Article
  9. Surface Analysis: From Single Crystals to Biomaterials.Surface and interface analysis : SIA · 2018
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors.

Tobias WeidnerNational ESCA and Surface Analysis Center for Biomedical Problems (NESAC/BIO), Department of Bioengineering, University of Washington, Seattle, WA 98195-1653, USA. weidner@mpip-mainz.mpg.de
David G Castner

Funding

Surface Analysis Facility for Biomedical ProblemsP41EB002027 · NIBIB · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G · 2003 to 2019
$17.6M
Protein-Crystal Molecular Recognition in BiomineralizationR01DE012554 · NIDCR · UNIVERSITY OF WASHINGTON · PI STAYTON, PATRICK S. · 1997 to 2012
$6.2M
Nanoscale Investigation of Protein-Surface InteractionsR01GM074511 · NIGMS · UNIVERSITY OF WASHINGTON · PI CASTNER, DAVID G · 2006 to 2009
$2.3M
NIBIB NIH HHS EB-002027NIBIB NIH HHS P41 EB002027NIDCR NIH HHS DE-012554NIDCR NIH HHS R01 DE012554NIGMS NIH HHS GM-074511NIGMS NIH HHS R01 GM074511
6 · The paper itself

Abstract

The surface of a material is rapidly covered with proteins once that material is placed in a biological environment. The structure and function of these bound proteins play a key role in the interactions and communications of the material with the biological environment. Thus, it is crucial to gain a molecular level understanding of surface bound protein structure. While X-ray diffraction and solution phase NMR methods are well established for determining the structure of proteins in the crystalline or solution phase, there is not a corresponding single technique that can provide the same level of structural detail about proteins at surfaces or interfaces. However, recent advances in sum frequency generation (SFG) vibrational spectroscopy have significantly increased our ability to obtain structural information about surface bound proteins and peptides. A multi-technique approach of combining SFG with (1) protein engineering methods to selectively introduce mutations and isotopic labels, (2) other experimental methods such as time-of-flight secondary ion mass spectrometry (ToF-SIMS) and near edge X-ray absorption fine structure (NEXAFS) to provide complementary information, and (3) molecular dynamic (MD) simulations to extend the molecular level experimental results is a particularly promising route for structural characterization of surface bound proteins and peptides. By using model peptides and small proteins with well-defined structures, methods have been developed to determine the orientation of both backbone and side chains to the surface.

Indexed as

Isotope LabelingMolecular Dynamics SimulationPeptidesPolystyrenesProteinsProtein Structure, SecondarySpectrometry, Mass, Secondary IonSurface PropertiesX-Ray Absorption SpectroscopyPeptidesPolystyrenesProteins

Identifiers

PMID23727992
PMCPMC3732458

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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.