[NMR paper] Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-molecule force spectroscopy (SMFS) has become a powerful tool in investigating the mechanical unfolding/folding of proteins at the single-molecule level. Polyproteins made of tandem identical repeats have been widely used in atomic force microscopy (AFM)-based SMFS studies, where polyproteins not only serve as fingerprints to identify single-molecule stretching events, but may also improve statistics of data...
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[NMR paper] Screening protein - single stranded RNA complexes by NMR spectroscopy for structure determination.
Screening protein - single stranded RNA complexes by NMR spectroscopy for structure determination.
Screening protein - single stranded RNA complexes by NMR spectroscopy for structure determination.
Methods. 2013 Oct 1;
Authors: Foot JN, Feracci M, Dominguez C
Abstract
In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory...
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Screening protein – single stranded RNA complexes by NMR spectroscopy for structure determination
Screening protein – single stranded RNA complexes by NMR spectroscopy for structure determination
Publication date: Available online 1 October 2013
Source:Methods</br>
Author(s): Jaelle N. Foot , Mikael Feracci , Cyril Dominguez</br>
In the past few years, RNA molecules have been revealed to be at the center of numerous biological processes. Long considered as passive molecules transferring genetic information from DNA to proteins, it is now well established that RNA molecules play important regulatory roles. Associated with that, the number of identified RNA...
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10-01-2013 11:15 PM
[NMR paper] A new sequence for single-shot diffusion-weighted NMR spectroscopy by the trace of the diffusion tensor.
A new sequence for single-shot diffusion-weighted NMR spectroscopy by the trace of the diffusion tensor.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles A new sequence for single-shot diffusion-weighted NMR spectroscopy by the trace of the diffusion tensor.
Magn Reson Med. 2012 Dec;68(6):1705-12
Authors: Valette J, Giraudeau C, Marchadour C, Djemai B, Geffroy F, Ghaly MA, Le Bihan D, Hantraye P, Lebon V, Lethimonnier F
...
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05-31-2013 11:16 AM
Oak Ridge, Berkeley research replication protein - UTDailyBeacon.com
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Oak Ridge, Berkeley research replication protein
UTDailyBeacon.com
"In order to get the whole picture, many different techniques are being used to study RPA, with important roles for x-ray crystallography, Nuclear Magnetic Resonance spectroscopy, small angle x-ray scattering and computer modeling. I brought the ...
Oak Ridge, Berkeley research replication protein - UTDailyBeacon.com
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02-05-2013 09:31 AM
[NMR paper] Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by N
Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Related Articles Comparison of Pf1 and Fd gene 5 proteins and their single-stranded DNA complexes by NMR spectroscopy and differential scanning calorimetry.
Biochemistry. 1995 Jan 10;34(1):148-54
Authors: Davis KG, Plyte SE, Robertson SR, Cooper A, Kneale GG
The Pf1 gene 5 protein forms a large helical nucleoprotein complex (Mr = 3.1 x 10(7)) with single-stranded viral DNA, from which a 32 amino acid...
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[NMR paper] Secondary structure of the single-stranded DNA binding protein encoded by filamentous
Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Secondary structure of the single-stranded DNA binding protein encoded by filamentous phage Pf3 as determined by NMR.
Eur J Biochem. 1994 Sep 1;224(2):663-76
Authors: Folmer RH, Folkers PJ, Kaan A, Jonker AJ, Aelen JM, Konings RN, Hilbers CW
Nuclear magnetic resonance...
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[NMR paper] Identification of the single-stranded DNA binding surface of the transcriptional coac
Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
J Biol Chem. 1999 Feb 5;274(6):3693-9
Authors: Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R
The C-terminal domain of the eukaryotic transcriptional cofactor PC4...