Related ArticlesA general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TOCSY triple resonance experiments.
J Biomol NMR. 1993 Mar;3(2):225-31
Authors: Logan TM, Olejniczak ET, Xu RX, Fesik SW
A general approach for assigning the resonances of uniformly 15N- and 13C-labeled proteins in their unfolded state is presented. The assignment approach takes advantage of the spectral dispersion of the amide nitrogen chemical shifts in denatured proteins by correlating side chain and backbone carbon and proton frequencies with the amide resonances of the same and adjacent residues. The 1H resonances of the individual amino acid spin systems are correlated with their intraresidue amide in a 3D 15N-edited 1H,1H-TOCSY-HSQC experiment, which allows the spin systems to be assigned to amino acid type. The spin systems are then linked to the adjacent i-1 spin system using the 3D H(C)(CO)NH-TOCSY experiment. Complete 13C assignments are obtained from the 3D (H)C(CO)NH-TOCSY experiment. Unlike other methods for assigning denatured proteins, this approach does not require previous knowledge of the native state assignments or specific interconversion rates between the native and denatured forms. The strategy is demonstrated by assigning the 1H, 13C, and 15N resonances of the FK506 binding protein denatured in 6.3 M urea.
Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids
Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids
Abstract Unravelling the complex correlation between chemical shifts of 13 C α, 13 C β, 13 C�, 1 H α, 15 N, 1 H N atoms in amino acids of proteins from NMR experiment and local structural environments of amino acids facilitates the assignment of secondary structures of proteins. This is an important impetus for both determining the three-dimensional structure and understanding the biological function of proteins. The previous...
nmrlearner
Journal club
0
11-14-2011 08:45 AM
Engineering [Ln(DPA)3]3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Engineering 3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Abstract Paramagnetic relaxation enhancements from unpaired electrons observed in nuclear magnetic resonance (NMR) spectra present powerful long-range distance restraints. The most frequently used paramagnetic tags, however, are tethered to the protein via disulfide bonds, requiring proteins with single cysteine residues for covalent attachment. Here we present a straightforward strategy to tag proteins site-specifically with paramagnetic lanthanides without a tether and...
[NMR paper] A general NMR method for rapid, efficient, and reliable biochemical screening.
A general NMR method for rapid, efficient, and reliable biochemical screening.
Related Articles A general NMR method for rapid, efficient, and reliable biochemical screening.
J Am Chem Soc. 2003 Nov 26;125(47):14620-5
Authors: Dalvit C, Ardini E, Flocco M, Fogliatto GP, Mongelli N, Veronesi M
High-throughput screening is usually the method of drug-lead discovery. It is now well accepted that, for a functional assay, quality is more important than quantity. The ligand-based or protein-based NMR screening methodologies for detecting compounds...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] A general method for determining the electron self-exchange rates of blue copper prot
A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
Related Articles A general method for determining the electron self-exchange rates of blue copper proteins by longitudinal NMR relaxation.
J Am Chem Soc. 2002 Apr 17;124(15):4093-6
Authors: Jensen MR, Hansen DF, Led JJ
A general NMR method is presented that allows a precise determination of the second-order rate constant, k(ese), for the electron self-exchange in blue copper proteins, from the longitudinal relaxation...
nmrlearner
Journal club
0
11-24-2010 08:49 PM
[NMR paper] Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets po
Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains.
Related Articles Assigning the NMR spectra of aromatic amino acids in proteins: analysis of two Ets pointed domains.
Biochem Cell Biol. 1998;76(2-3):379-90
Authors: Slupsky CM, Gentile LN, McIntosh LP
The measurement of interproton nuclear Overhauser enhancements (NOEs) and dihedral angle restraints of aromatic amino acids is a critical step towards determining the structure of a protein. The complete assignment of the resonances from aromatic...
A general method for assigning NMR spectra of denatured proteins using 3D HC(CO)NH-TO
Linear Mode
