Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Abstract Random coil chemical shifts are necessary for secondary chemical shift analysis, which is the main NMR method for identification of secondary structure in proteins. One of the largest challenges in the determination of random coil chemical shifts is accounting for the effect of neighboring residues. The contributions from the neighboring residues are typically removed by using neighbor correction factors determined based on each...
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06-06-2011 12:53 AM
[NMR paper] Phosphate ions in bone: identification of a calcium-organic phosphate complex by 31P
Phosphate ions in bone: identification of a calcium-organic phosphate complex by 31P solid-state NMR spectroscopy at early stages of mineralization.
Related Articles Phosphate ions in bone: identification of a calcium-organic phosphate complex by 31P solid-state NMR spectroscopy at early stages of mineralization.
Calcif Tissue Int. 2003 May;72(5):610-26
Authors: Wu Y, Ackerman JL, Strawich ES, Rey C, Kim HM, Glimcher MJ
Previous 31P cross-polarization and differential cross-polarization magic angle spinning (CP/MAS and DCP/MAS) solid-state NMR...
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11-24-2010 09:01 PM
[NMR paper] Sequence-dependent correction of random coil NMR chemical shifts.
Sequence-dependent correction of random coil NMR chemical shifts.
Related Articles Sequence-dependent correction of random coil NMR chemical shifts.
J Am Chem Soc. 2001 Apr 4;123(13):2970-8
Authors: Schwarzinger S, Kroon GJ, Foss TR, Chung J, Wright PE, Dyson HJ
Random coil chemical shifts are commonly used to detect secondary structure elements in proteins in chemical shift index calculations. While this technique is very reliable for folded proteins, application to unfolded proteins reveals significant deviations from measured random coil...
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11-19-2010 08:32 PM
Characterization of (1)H NMR signal in human cortical bone for magnetic resonance ima
Characterization of (1)H NMR signal in human cortical bone for magnetic resonance imaging.
Characterization of (1)H NMR signal in human cortical bone for magnetic resonance imaging.
Magn Reson Med. 2010 Sep;64(3):680-7
Authors: Horch RA, Nyman JS, Gochberg DF, Dortch RD, Does MD
Recent advancements in MRI have enabled clinical imaging of human cortical bone, providing a potentially powerful new means for assessing bone health with molecular-scale sensitivities unavailable to conventional X-ray-based diagnostics. In human cortical bone, MRI is...
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09-02-2010 03:58 PM
[NMR paper] Correction of the NMR structure of the ETS1/DNA complex.
Correction of the NMR structure of the ETS1/DNA complex.
Related Articles Correction of the NMR structure of the ETS1/DNA complex.
J Biomol NMR. 1997 Dec;10(4):317-28
Authors: Werner MH, Clore GM, Fisher CL, Fisher RJ, Trinh L, Shiloach J, Gronenborn AM
The ETS family of transcription factors consists of a group of proteins that share a highly conserved 85 amino acid DNA-binding domain (DBD). This family recognizes a consensus sequence rich in purine bases with a central GGAA motif. A comparison of the published three-dimensional structures of...
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08-22-2010 05:08 PM
[NMR paper] How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR s
How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
Related Articles How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X.
J Biol Chem. 1992 Sep 25;267(27):19642-9
Authors: Selander-Sunnerhagen M, Ullner M, Persson E, Teleman O, Stenflo J, Drakenberg T
Domains homologous to the epidermal growth factor...
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08-21-2010 11:45 PM
Automated solvent artifact removal and base plane correction of multidimensional NMR
Abstract Strong solvent signals lead to a disappearance of weak protein signals close to the solvent resonance frequency and to base plane variations all over the spectrum. AUREMOL-SSA provides an automated approach for solvent artifact removal from multidimensional NMR protein spectra. Its core algorithm is based on singular spectrum analysis (SSA) in the time domain and is combined with an automated base plane correction in the frequency domain. The performance of the method has been tested on synthetic and experimental spectra including two-dimensional NOESY and TOCSY spectra and a...
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08-14-2010 04:19 AM
CheckShift: automatic correction of inconsistent chemical shift referencing
CheckShift: automatic correction of inconsistent chemical shift referencing
Simon W. Ginzinger, Fabian Gerick, Murray Coles and Volker Heun
Journal of Biomolecular NMR; 2007; 39(3); pp 223-227
Abstract:
The construction of a consistent protein chemical shift database is an important step toward making more extensive use of this data in structural studies. Unfortunately, progress in this direction has been hampered by the quality of the available data, particularly with respect to chemical shift referencing, which is often either inaccurate or inconsistently annotated. Preprocessing of...
Correction for Fujita et al., Bone marrow transplantation restores epidermal basement
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