[ASAP] Single-Molecule Imaging Reveals Conformational Manipulation of Holliday Junction DNA by the Junction Processing Protein RuvA
Single-Molecule Imaging Reveals Conformational Manipulation of Holliday Junction DNA by the Junction Processing Protein RuvA
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00404/20180524/images/medium/bi-2018-00404a_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00404
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05-25-2018 12:07 PM
[NMR paper] 3D 14N/1H Double Quantum/1H Single Quantum Correlation Solid-State NMR for Probing Parallel and Anti-Parallel Beta-Sheet Arrangement of Oligo-Peptides at Natural Abundance.
3D 14N/1H Double Quantum/1H Single Quantum Correlation Solid-State NMR for Probing Parallel and Anti-Parallel Beta-Sheet Arrangement of Oligo-Peptides at Natural Abundance.
Related Articles 3D 14N/1H Double Quantum/1H Single Quantum Correlation Solid-State NMR for Probing Parallel and Anti-Parallel Beta-Sheet Arrangement of Oligo-Peptides at Natural Abundance.
Chemphyschem. 2018 May 08;:
Authors: Hong YL, Asakura T, Nishiyama Y
Abstract
?-sheet structure of oligo- and poly-peptides can be formed in anti-parallel (AP)- and...
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05-09-2018 02:49 AM
[ASAP] Watching Three-Dimensional Movements of Single Membrane Proteins in Lipid Bilayers
Watching Three-Dimensional Movements of Single Membrane Proteins in Lipid Bilayers
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00253/20180412/images/medium/bi-2018-00253y_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00253
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04-13-2018 01:15 AM
Sequential DNA Binding and Dimerization Processesof the Photosensory Protein EL222
Sequential DNA Binding and Dimerization Processesof the Photosensory Protein EL222
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01206/20180219/images/medium/bi-2017-01206b_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01206
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02-21-2018 12:45 AM
[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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12-27-2016 11:04 PM
[NMR paper] Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
Related Articles Complete backbone and DENQ side chain NMR assignments in proteins from a single experiment: implications to structure-function studies.
J Struct Funct Genomics. 2014 Feb 18;
Authors: Reddy JG, Hosur RV
Abstract
Resonance assignment is the first and the most crucial step in all nuclear magnetic resonance (NMR) investigations on structure-function relationships in biological...
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02-19-2014 03:12 PM
[NMR paper] NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
J Phys Chem B. 2012 Dec 13;116(49):14207-15
Authors: Sonti R, Rai R, Ragothama S, Balaram P
Abstract
Cross strand aromatic interactions between a facing pair of...
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06-13-2013 06:14 PM
Solid-state NMR analysis of the ?-strand orientation of the protofibrils of amyloid ?-protein
Solid-state NMR analysis of the ?-strand orientation of the protofibrils of amyloid ?-protein
30 November 2012
Publication year: 2012
Source:Biochemical and Biophysical Research Communications, Volume 428, Issue 4</br>
</br>
Alzheimer’s disease (AD) is caused by abnormal deposition (fibrillation) of a 42-residue amyloid ?-protein (A?42) in the brain. During the process of fibrillation, the A?42 takes the form of protofibrils with strong neurotoxicity, and is thus believed to play a crucial role in the pathogenesis of AD. To elucidate the supramolecular structure of the...