Evidence map›Paper›PMID 30549169›Full record

ArticleAngewandte Chemie (International ed. in English)2019

Surface Attachment Enhances the Thermodynamic Stability of Protein L.

Gabriel Ortega, Martin Kurnik, Philippe Dauphin-Ducharme, Hui Li, Netzahualcóyotl Arroyo-Currás, Amanda Caceres, Kevin W Plaxco

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

7 authors.

Gabriel OrtegaDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0002-7126-9096
Martin KurnikDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0001-9255-9730
Philippe Dauphin-DucharmeDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0002-0490-7115
Hui LiDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0001-7849-9735
Netzahualcóyotl Arroyo-CurrásDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0002-2740-6276
Amanda CaceresDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0001-8706-7547
Kevin W PlaxcoDepartment of Chemistry and Biochemistry, University of California Santa Barbara, Santa Barbara, CA, 93106, USA.ORCID 0000-0003-4772-8771

Funding

The thermodynamics of protein-surface interactionsR01GM118560 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PLAXCO, KEVIN W · 2017 to 2020
$1.4M
Bio-Optical Composites for Rapid Analyte DetectionR01GM062958 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PLAXCO, KEVIN W. · 2001 to 2002
$428k
A new tool for measuring surface-biomolecule interactionsR21EB018617 · NIBIB · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI PLAXCO, KEVIN W · 2014 to 2015
$409k
NIBIB NIH HHS R21 EB018617NIGMS NIH HHS R01 GM062958NIGMS NIH HHS R01 GM118560
6 · The paper itself

Abstract

Despite the importance of protein-surface interactions in both biology and biotechnology, our understanding of their origins is limited due to a paucity of experimental studies of the thermodynamics behind such interactions. In response, we have characterized the extent to which interaction with a chemically well-defined macroscopic surface alters the stability of protein L. To do so, we site-specifically attached a redox-reporter-modified protein variant to a hydroxy-terminated monolayer on a gold surface and then used electrochemistry to monitor its guanidine denaturation and determine its folding free energy. Comparison with the free energy seen in solution indicates that interaction with this surface stabilizes the protein by 6 kJ mol

Indexed as

ThermodynamicsElectrochemical TechniquesGoldProtein FoldingProteinsProtein StabilityStatic ElectricitySurface PropertiesGoldProteinsbiophysicselectrochemistryprotein engineeringproteinsthermodynamics

Identifiers

PMID30549169
PMCPMC6512982

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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.