[NMR paper] Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Related Articles Chiral discrimination of ?-hydroxy acids and N-Ts-?-amino acids induced by tetraaza macrocyclic chiral solvating agents by using (1)H NMR spectroscopy.
Org Biomol Chem. 2017 Jan 27;:
Authors: Lv C, Feng L, Zhao H, Wang G, Stavropoulos P, Ai L
Abstract
In the field of chiral recognition, reported chiral discrimination by (1)H NMR spectroscopy has mainly focused on...
pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements
pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements
Abstract
The pK a values and charge states of ionizable residues in polypeptides and proteins are frequently determined via NMR-monitored pH titrations. To aid the interpretation of the resulting titration data, we have measured the pH-dependent chemical shifts of nearly all the 1H, 13C, and 15N nuclei in the seven common ionizable amino acids (XÂ*=Â*Asp, Glu, His, Cys, Tyr, Lys, and Arg)...
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[NMR paper] Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.
J Biomol NMR. 2013 Aug 14;
Authors: Bellstedt P, Seiboth T, Häfner S, Kutscha H, Ramachandran R, Görlach M
Abstract
NMR-based structure determination of a protein requires the assignment of resonances as indispensable first step. Even though...
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VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
Abstract Homology modeling is a powerful tool for predicting protein structures, whose success depends on obtaining a reasonable alignment between a given structural template and the protein sequence being analyzed. In order to leverage greater predictive power for proteins with few structural templates, we have developed a method to rank homology models based upon their compliance to secondary structure derived from experimental solid-state NMR...
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12-22-2011 06:50 AM
[NMR paper] Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic stu
Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Related Articles Phosphorylated amino acids: model compounds for solid-state 31P NMR spectroscopic studies of proteins.
Magn Reson Chem. 2004 Apr;42(4):369-72
Authors: Iuga A, Brunner E
Solid-state 31P NMR spectroscopy was applied to measure the isotropic chemical shifts, chemical shift anisotropies and asymmetry parameters of three phosphorylated amino acids, O-phospho-L-serine, O-phospho-L-threonine and O-phospho-L-tyrosine. The...
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11-24-2010 09:51 PM
[NMR paper] 14N NMR relaxation times of several protein amino acids in aqueous solution--comparis
14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.
Related Articles 14N NMR relaxation times of several protein amino acids in aqueous solution--comparison with 17O NMR data and estimation of the relative hydration numbers in the cationic and zwitterionic forms.
J Magn Reson. 2003 Oct;164(2):294-303
Authors: Troganis AN, Tsanaktsidis C, Gerothanassis IP
The 14N nuclear magnetic resonance (NMR)...
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[NMR paper] Comparison between the phi distribution of the amino acids in the protein database an
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation.
J Mol Biol. 1995 Nov 24;254(2):322-33
Authors: Serrano L
...
Model learns how individual amino acids determine protein function - The MIT Tech
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