Andreas, L. B., Jaudzems, K., Stanek, J., Lalli, D., Bertarello, A., Le Marchand, T., Cala-De Paepe, D., Kotelovica, S., Akopjana, I., Knott, B., Wegner, S., Engelke, F., Lesage, A., Emsley, L., Tars, K., Herrmann, T., Pintacuda, G....
Date: 2016-08-16
Protein structure determination by proton-detected magic-angle spinning (MAS) NMR has focused on highly deuterated samples, in which only a small number of protons are introduced and observation of signals from side chains is extremely limited. Here, we show in two fully protonated proteins that, at 100-kHz MAS and above, spectral... Read More
PNAS:
Number: 33
Volume: 113
Did you find this post helpful? |
Similar Threads
Thread
Thread Starter
Forum
Replies
Last Post
DNP MAS NMR on channelrhodopsin-2 [Biophysics and Computational Biology]
DNP MAS NMR on channelrhodopsin-2
Becker-Baldus, J., Bamann, C., Saxena, K., Gustmann, H., Brown, L. J., Brown, R. C. D., Reiter, C., Bamberg, E., Wachtveitl, J., Schwalbe, H., Glaubitz, C....
Date: 2015-08-11
Channelrhodopsin-2 from Chlamydomonas reinhardtii is a light-gated ion channel. Over recent years, this ion channel has attracted considerable interest because of its unparalleled role in optogenetic applications. However, despite considerable efforts, an understanding of how molecular events during the photocycle, including the retinal trans-cis isomerization and the...
nmrlearner
Journal club
0
08-12-2015 08:58 AM
Protein dynamics from X-ray and NMR [Biophysics and Computational Biology]
Protein dynamics from X-ray and NMR
Fenwick, R. B., van den Bedem, H., Fraser, J. S., Wright, P. E....
Date: 2014-01-28
Detailed descriptions of atomic coordinates and motions are required for an understanding of protein dynamics and their relation to molecular recognition, catalytic function, and allostery. Historically, NMR relaxation measurements have played a dominant role in the determination of the amplitudes and timescales (picosecond–nanosecond) of bond vector fluctuations, whereas high-resolution X-ray... Read More
PNAS:
Number: 4
nmrlearner
Journal club
0
01-29-2014 12:50 AM
Crystal and NMR structures of a Trp-cage [Biophysics and Computational Biology]
Crystal and NMR structures of a Trp-cage
Scian, M., Lin, J. C., Le Trong, I., Makhatadze, G. I., Stenkamp, R. E., Andersen, N. H....
Date: 2012-07-31
To provide high-resolution X-ray crystallographic structures of a peptide with the Trp-cage fold, we prepared a cyclized version of this motif. Cyclized Trp-cage is remarkably stable and afforded two crystal forms suitable for X-ray diffraction. The resulting higher resolution crystal structures validate the prior NMR models and provide explanations for experimental observations that could not be rationalized by NMR structural data,...
nmrlearner
Journal club
0
07-31-2012 08:27 PM
Protein structure modeling using sparse NMR data [Biophysics and Computational Biology]
Protein structure modeling using sparse NMR data
Thompson, J. M., Sgourakis, N. G., Liu, G., Rossi, P., Tang, Y., Mills, J. L., Szyperski, T., Montelione, G. T., Baker, D....
Date: 2012-06-19
While information from homologous structures plays a central role in X-ray structure determination by molecular replacement, such information is rarely used in NMR structure determination because it can be incorrect, both locally and globally, when evolutionary relationships are inferred incorrectly or there has been considerable evolutionary structural divergence. Here we describe a method that...
nmrlearner
Journal club
0
06-20-2012 02:28 AM
Ultrahigh resolution protein structures using NMR chemical shift tensors [Biophysics and Computational Biology]
Ultrahigh resolution protein structures using NMR chemical shift tensors
Wylie, B. J., Sperling, L. J., Nieuwkoop, A. J., Franks, W. T., Oldfield, E., Rienstra, C. M....
Date: 2011-10-11
NMR chemical shift tensors (CSTs) in proteins, as well as their orientations, represent an important new restraint class for protein structure refinement and determination. Here, we present the first determination of both CST magnitudes and orientations for 13C? and 15N (peptide backbone) groups in a protein, the ?1 IgG binding domain of protein G from Streptococcus spp., GB1. Site-specific 13C? and...
nmrlearner
Journal club
0
10-12-2011 06:37 AM
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR [Biophysics and Computational Biology]
Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR
Kato, H., van Ingen, H., Zhou, B.-R., Feng, H., Bustin, M., Kay, L. E., Bai, Y....
Date: 2011-07-26
Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility group nucleosomal (HMGN) protein family that regulates various chromatin functions, including transcription. Here, we report the architecture of the HMGN2-nucleosome...
nmrlearner
Journal club
0
07-26-2011 11:22 PM
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion [Biophysics and Computational Biology]
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion
Meinhold, D. W., Wright, P. E....
Date: 2011-05-31
Detailed understanding of protein function and malfunction hinges on the ability to characterize transiently populated states and the transitions between them. Here, we use 15N, , and 13CO NMR R2 relaxation dispersion to investigate spontaneous unfolding and refolding events of native apomyoglobin. Above pH 5.0, dispersion is dominated by processes involving fluctuations of the F-helix region, which...
nmrlearner
Journal club
0
05-31-2011 11:41 PM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy [Biophysics and Computational Biology]
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy
Masterson, L. R., Shi, L., Metcalfe, E., Gao, J., Taylor, S. S., Veglia, G....
Date: 2011-04-26
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states (open, intermediate, and closed) that are dynamically and allosterically activated by nucleotide binding. We show that the structural transitions between these...
![Protein NMR structures at >=100-kHz MAS [Biophysics and Computational Biology]](http://www.bionmr.com/forum/iconimages/journal-club-9/protein-nmr-structures-%3D100-khz-mas-%5Bbiophysics-computational-biology%5D_ltr.gif)
Protein NMR structures at >=100-kHz MAS [Biophysics and Computational Biology]
Linear Mode
