Evidence map›Paper›PMID 26266832›Full record

ArticleChemphyschem : a European journal of chemical physics and physical chemistry2015

Biosilica-Entrapped Enzymes Studied by Using Dynamic Nuclear-Polarization-Enhanced High-Field NMR Spectroscopy.

Enrico Ravera, Vladimir K Michaelis, Ta-Chung Ong, Eric G Keeler, Tommaso Martelli, Marco Fragai, Robert G Griffin, Claudio Luchinat

Open access · greenAbstract read
In one paragraph

Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
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

11 citing papers in PubMed, 41 citations in OpenAlex.

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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

8 authors at 4 institutions in 3 countries.

Enrico RaveraMagnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino (FI) (Italy).
Vladimir K MichaelisFrancis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139 (USA).
Ta-Chung OngFrancis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139 (USA).
Eric G KeelerFrancis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139 (USA).
Tommaso MartelliMagnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino (FI) (Italy).
Marco FragaiMagnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino (FI) (Italy).
Robert G GriffinFrancis Bitter Magnet Laboratory and Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139 (USA).
Claudio LuchinatMagnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino (FI) (Italy).
Massachusetts Institute of Technology · USInteruniversity Consortium for Magnetic Resonance · ITUniversity of Florence · ITETH Zurich · CH

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
High Field DNP in Biological SystemsR01EB002804 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$9.1M
Solid State NMR Studies of Peptides and ProteinsR01EB003151 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2004 to 2015
$6.5M
800 MHz Low Temperature Magic Angle Spinning NMR Probe.S10RR027895 · NCRR · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2009 to 2009
$300k
NCRR NIH HHS S10 RR027895NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB002804NIBIB NIH HHS R01 EB003151
6 · The paper itself

Abstract

Enzymes are used as environmentally friendly catalysts in many industrial applications, and are frequently immobilized in a matrix to improve their chemical stability for long-term storage and reusability. Recently, it was shown that an atomic-level description of proteins immobilized in a biosilica matrix can be attained by examining their magic-angle spinning (MAS) NMR spectra. However, even though MAS NMR is an excellent tool for determining structure, it is severely hampered by sensitivity. In this work we provide the proof of principle that NMR characterization of biosilica-entrapped enzymes could be assisted by high-field dynamic nuclear polarization (DNP).

Indexed as

biomaterialsbiosilicaDNPenzyme immobilizationsolid-state NMR

Identifiers

PMID26266832
PMCPMC4752418
OpenAlexW2159737424

What OpenQuestion holds

Textmetadata
LicenceTDM
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.