Disordered proteins studied by chemical shifts
Disordered proteins studied by chemical shifts
January 2012
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 60</br>
</br>
</br>
</br></br>
nmrlearner
Journal club
0
12-01-2012 06:10 PM
4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
4D Non-uniformly sampled HCBCACON and 1J(NCα)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
Abstract A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit 13C direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (Hα, and Hβ) and carbon (Cα, Cβ) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient...
nmrlearner
Journal club
0
05-17-2012 08:40 AM
Disordered proteins studied by chemical shifts
Disordered proteins studied by chemical shifts
Publication year: 2012
Source:Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 60</br>
Magnus Kjaergaard, Flemming M. Poulsen</br>
</br>
</br></br>
nmrlearner
Journal club
0
03-09-2012 09:16 AM
Disordered proteins studied by chemical shifts
Disordered proteins studied by chemical shifts
Publication year: 2011
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, Available online 12 October 2011</br>
Magnus*Kjaergaard, Flemming M.*Poulsen</br>
More...
nmrlearner
Journal club
0
10-14-2011 07:16 AM
Structure-based prediction of methyl chemical shifts in proteins
Structure-based prediction of methyl chemical shifts in proteins
Abstract Protein methyl groups have recently been the subject of much attention in NMR spectroscopy because of the opportunities that they provide to obtain information about the structure and dynamics of proteins and protein complexes. With the advent of selective labeling schemes, methyl groups are particularly interesting in the context of chemical shift based protein structure determination, an approach that to date has exploited primarily the mapping between protein structures and backbone chemical shifts. In order to...
nmrlearner
Journal club
0
07-15-2011 09:10 PM
Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH
Abstract Secondary chemical shift analysis is the main NMR method for detection of transiently formed secondary structure in intrinsically disordered proteins. The quality of the secondary chemical shifts is dependent on an appropriate choice of random coil chemical shifts. We report random coil chemical shifts and sequence correction factors determined for a GGXGG peptide series following the approach of Schwarzinger et al. (J Am Chem Soc 123(13):2970â??2978, 2001). The chemical shifts are...
nmrlearner
Journal club
0
01-17-2011 02:40 AM
[NMR paper] NMR chemical shifts and structure refinement in proteins.
NMR chemical shifts and structure refinement in proteins.
Related Articles NMR chemical shifts and structure refinement in proteins.
J Biomol NMR. 1993 Sep;3(5):607-12
Authors: Laws DD, de Dios AC, Oldfield E
Computation of the 13C alpha chemical shifts (or shieldings) of glycine, alanine and valine residues in bovine and Drosophila calmodulins and Staphylococcal nuclease, and comparison with experimental values, is reported using a gauge-including atomic orbital quantum-chemical approach. The full approximately 24 ppm shielding range is...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
Analysis of and chemical shifts of cysteine and cystine residues in proteins: a quant
Abstract Cysteines possess a unique property among the 20 naturally occurring amino acids: it can be present in proteins in either the reduced or oxidized form, and can regulate the activity of some proteins. Consequently, to augment our previous treatment of the other types of residues, the
13\textC\upalpha and
13\textC\upbeta chemical shifts of 837 cysteines in disulfide-bonded cystine from a set of seven non-redundant proteins, determined by X-ray crystallography and NMR spectroscopy, were computed at the DFT level of theory. Our results indicate that the errors between observed...