Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease.
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Summary
The use of novel two-dimensional nuclear magnetic resonance (NMR) pulse sequences to provide insight into protein dynamics is described, suggesting that there is no correlation between these rapid small amplitude motions and secondary structure for S. Nase.
- Type
- article
- Published
- 1989-11-14
- Cited by
- 1,802
- References
- 59
- OpenAlex
- https://openalex.org/W2086862822
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:15292815
Keywords
Heteronuclear molecule, Homonuclear molecule, Chemistry, Nuclear Overhauser effect, Nuclear magnetic resonance spectroscopy
References
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- Pulse sequences utilizing the correlated motion of coupled heteronuclei in the transverse plane of the doubly rotating frame
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- Backbone dynamics of a model membrane protein: 13C NMR spectroscopy of alanine methyl groups in detergent-solubilized M13 coat protein.
- NMR relaxation study of internal motions in Staphylococcal nuclease
- Rotational Spectral Density Functions for Aqueous Sucrose: Experimental Determination Using 13C NMR
- Enhancement of nuclear magnetic resonance signals by polarization transfer
- Determination of 15N chemical shift tensor via 15N-2H dipolar coupling in Boc-glycylglycyl[15N]glycine benzyl ester
- Nuclear Overhauser Effects and 13C Relaxation Times in 13C–H Double Resonance Spectra
- Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
- Theory for nuclear magnetic relaxation of probes in anisotropic systems: application of cholesterol in phospholipid vesicles.
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- Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements.
- Molecular simulations of conformational transitions in biomolecules using a novel computational tool
- Propagation of experimental uncertainties using the Lipari-Szabo model-free analysis of protein dynamics
- Structure of C-terminal Domain of Parkin, IBR-RING2
- Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer.
- Comparison of 15N- and 13C-determined parameters of mobility in melittin
- Spectral density function mapping using 15N relaxation data exclusively
- Backbone dynamics of a domain of protein L which binds to immunoglobulin light chains.
- Local protein instability predictive of helper T-cell epitopes.
- NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer β-sheet
- Yeast Transcript Elongation Factor (TFIIS), Structure and Function
- How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.
- Solution Structure of the ε Subunit of the F1-ATPase from Escherichia coli and Interactions of This Subunit with β Subunits in the Complex*
- Arginine side-chain dynamics in the HIV-1 rev-RRE complex.
- Solution structure and backbone dynamics of an antigen‐free heavy chain variable domain (VHH) from Llama
- Structure of domain III of the blood-stage malaria vaccine candidate, Plasmodium falciparum apical membrane antigen 1 (AMA1).
- Characterization and manipulation of the Pseudomonas aeruginosa dimethylarginine dimethylaminohydrolase monomer--dimer equilibrium.
- Cell‐free expression and selective isotope labelling in protein NMR
- Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease.
- Interaction of the C-Terminal Domains of Sendai Virus N and P Proteins: Comparison of Polymerase-Nucleocapsid Interactions within the Paramyxovirus Family
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