Theories of chemical shift anisotropies in proteins and nucleic acids

Sitkoff, Doree; Case, David A.

doi:10.1016/s0079-6565(98)00013-2

Cited by 172 publications

(167 citation statements)

References 99 publications

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“…Methods for automatic sequential assignment based on the use of 15 N connectivities observed on HNN and HN(C)N experiments were proposed [47], based on the different typical peak patterns observed in these experiments. The computational complexity of the sequential assignment problem using only 13 C chemical shift data and C (i, i -1) sequential connectivity information was explored [48].…”

Section: Spectral Assignmentmentioning

confidence: 99%

“…A strategy based on the RDCs was proposed [116] to simultaneously assign the spectral resonances and determine the structure. Another approach [117] is based on the measurement of sequential resonances between amide 1 H and 15 N and 13 C (corresponding to the intra-residue and to the sequential connectivities), along with 13 Ca-H dipolar couplings. This single-step determination of protein structure is intended to provide an efficient tool for the structure determination in structural proteomics.…”

Section: Dipolar Coupling Restraintsmentioning

confidence: 99%

“…A database of experimental chemical shifts was used along with homology of amino-acid triplets [161] to extract and angle restraints from the measured chemical shifts of backbone atoms. From the statistics on the 13 C chemical shifts, the conformation of the peptidic bond Xaa-Pro could be predicted [162]. The effect of sequence in the random coil chemical shift values was also statistically analyzed [163].…”

Section: Chemical Shift Restraintsmentioning

confidence: 99%

“…(i) The parameters measured by NMR are qualitatively very different from the electronic density from which the crystallographic structures are determined, and the scientific knowledge accumulated in X-ray crystallography cannot thus be transferred directly to NMR. (ii) The relationship between the geometrical and the NMR *Address correspondence to this authors at the Laboratoire de Biochimie Théorique, CNRS UPR 9080, Institut de Biologie PhysicoChimique, 13 parameters is fuzzy, because each NMR parameter is depending not only on the structure, but also on the internal dynamics of the molecule, and these two aspects are difficult to separate.…”

Section: Introductionmentioning

confidence: 99%

“…11 is presenting methods for structure and assignment determination using dipolar couplings. Two reviews are presenting the interpretation of chemical shifts and coupling constants in macromolecules [12] and the theory of chemical shift anisotropy [13].…”

Section: Introductionmentioning

confidence: 99%

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Quantitative Analysis of Biomolecular NMR Spectra: A Prerequisite for the Determination of the Structure and Dynamics of Biomolecules

Malliavin

2006

COC

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Nuclear Magnetic Resonance (NMR) became during the two last decades an important method for biomolecular structure determination. NMR permits to study biomolecules in solution and gives access to the molecular flexibility at atomic level on a complete structure: in that respect, it is occupying a unique place i n structural biology. During the first years of its development, NMR was trying to meet the requirements previously defined in X-ray crystallography. But, NMR then started to determine its own criteria for the definition of a structure. Indeed, the atomic coordinates of an NMR structure are calculated using restraints on geometrical parameters (angles and distances) of the structure, which are only indirectly related to atom positions: in that respect, NMR and X-ray crystallography are very different. The indirect relation between the NMR measurements and the molecular structure and dynamics makes critical the precision and the interpretation of the NMR parameters and the development of quantitative analysis methods. The methods published since 1997 for liquid-NMR of proteins are reviewed here. First, methods for structure determination are presented, as well as methods for spectral assignment and for structure quality assessment. Second, the quantitative analysis of structure mobility i s reviewed.

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