Proteins side chain resonances

Automated NMR Assignment of Protein Side Chain Resonances... 

Hiller S, Joss R, Wider G (2008) Automated NMR assignment of protein side chain resonances using automated projection spectroscopy (APSY). J Am Chem Soc 130 12073-12079... 

Jiang L, Coggins BE, Zhou P (2005) Rapid assignment of protein side chain resonances using projection-reconstruction of (4,3)D HC(CCO)NH and intra-HC(C)NH experiments. J Magn Reson 175 170-176... 

The Fe-N mode is at 222 in the R state and 207 cnY in the T state for the a subunits, but only shifted to 218 T state for the (3 subunits. This is consistent with the interpretation that the Fe-imidazole interations are weakened more in the T state of the a subunits than p subunits. Time-resolved resonance Raman studies have shown that the R T switch is complete on a 10 ps tuuescale [38]. Finally, UV excitation of the aromatic protein side chains yields... 

Solid state 13C CPMAS NMR spectra of Wheat High Molecular Weight (W.HMW) subunits show well resolved resonances identical with spectra of dry protein and peptide samples [24], Most of the amino acids side-chain resonances are found in the 0-35 ppm region followed by the alpha resonances of the most abundant amino acids glycine, glutamine and proline at chemical shifts of 42, 52 and 60 ppm, respectively, and the carbonyl carbons show a broad peak in 172-177 ppm region. The CPMAS spectra of hydrated whole HMW provides important information on the structural characteristics. 

A solution structure of French Bean plastocyanin has been reported by Wright and co-workers,19 using nuclear magnetic resonance techniques described in Section 3.5 of Chapter 3. The structure, determined from a plastocyanin molecule in solution rather than in a solid-state crystal, agrees well with that of reduced poplar plastocyanin X-ray crystallographic structure reported above. Conformations of protein side chains constituting the hydrophobic core of the French bean plastocyanin are well-defined by the NMR technique. Surface side chains show... 

An important factor in the structure of protein-DNA complexes can be the peptide backbone. The amide bond can fimction as an H-bond acceptor as well an H-bond donor. Due to the reduced flexibility of the backbone vs. side chain (resonance stabilization of the peptide bond), H-bonds to the peptide backbone lead to a rigid and tight arrangement in the complex and contribute extensively to the exact fit between protein and nucleic acid. 

Triple Resonance Experiments for Protein Side Chain Assignment 304... 

Keywords APSY Automated peak picking Automated resonance assignment GAPRO NMR Projection spectroscopy Protein backbone Protein side chains... 

Grzesiek S, Anglister J, Bax A (1993) Correlation of backbone amide and aliphatic side-chain resonances in C/ N-enriched proteins by isotropic mixing of C magnetization. J Magn Reson B 101 114-119... 

The following is a description of a typical run reported in scientific journals with computer-assisted NMR research (attention should be paid to the language of description) NMR experiments are carried out at 35°C on 600, 750, 800, and 900-MHz spectrometers, respectively. Proton, N, and, backbone and side-chain resonances of proteins are assigned by three-dimensional (3D) double- and triple-resonance NMR experiments H resonance for a protein by two-dimensional (2D) C-filtered experiments and P resonance of a protein from a 2D H- P correlation spectmm. 

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