Evidence map›Paper›PMID 24972273›Full record

ArticleMolecules (Basel, Switzerland)2014

Using MUSIC and CC(CO)NH for backbone assignment of two medium-sized proteins not fully accessible to standard 3D NMR.

Annette K Brenner, Nils Åge Frøystein

Abstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2014. 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

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2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

2 authors.

Annette K BrennerDepartment of Chemistry, University of Bergen, PO Box 7800, 5020 Bergen, Norway. annette.brenner@k2.uib.no.
Nils Åge FrøysteinDepartment of Chemistry, University of Bergen, PO Box 7800, 5020 Bergen, Norway. nils.froystein@kj.uib.no.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The backbone assignment of medium-sized proteins is rarely as straightforward as that of small proteins, and thus often requires creative solutions. Here, we describe the application of a combination of standard 3D heteronuclear methods with CC(CO)NH and a variety of MUltiplicity Selective In-phase Coherence transfer (MUSIC) experiments. Both CC(CO)NH and MUSIC are, in theory, very powerful methods for the backbone assignment of proteins. Due to low sensitivity, their use has usually been linked to small proteins only. However, we found that combining CC(CO)NH and MUSIC experiments simplified the assignment of two challenging medium-sized proteins of 13 and 19.5 kDa, respectively. These methods are to some extent complementary to each other: CC(CO)NH acquired with a long isotropic mixing time can identify amino acids with large aliphatic side chains. Whereas the most sensitive MUSIC experiments identify amino acid types that cannot be detected by CC(CO)NH, comprising the residues with acid and amide groups, and aromatic rings in their side chains. Together these methods provide a means of identifying the majority of peaks in the 2D 15N HSQC spectrum which simplifies the backbone assignment work even for proteins, e.g., small kinases, whose standard spectra resulted in little spectral resolution and low signal intensities.

Indexed as

HumansN-Terminal Acetyltransferase ENuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProtein Structure, TertiaryUbiquitinNAA50 protein, humanN-Terminal Acetyltransferase EUbiquitin

Identifiers

PMID24972273
PMCPMC6270747

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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.