The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
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Summary
This new method for rapidly and quantitatively determining the identity, extent, and location of secondary structural elements in proteins based on the simple inspection of the alpha-CH 1H resonance assignments is found to be almost as accurate as the more traditional NOE-based methods of determining secondary structure.
- Type
- article
- Published
- 1992-02-18
- Cited by
- 1,926
- References
- 23
- OpenAlex
- https://openalex.org/W2088848851
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31239769
Keywords
Nuclear magnetic resonance spectroscopy, Chemical shift, Simple (philosophy), Chemistry, Spectroscopy
References
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- Peptide group shifts
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- The relationship between chemical shift and secondary structure in proteins
- Nuclear magnetic resonance studies of helix-coil transitions in polyamino acids.
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- 1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin.
- Nuclear magnetic resonance study of the globular domain of chicken histone H5: resonance assignment and secondary structure.
- Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy.
- α-Proton chemical shifts and secondary structure in proteins
- Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
- Sequence-specific 1H NMR assignment and secondary structure of the Arc repressor of bacteriophage P22, as determined by two-dimensional 1H NMR spectroscopy.
- Magnetic resonance studies of macromolecules. I. Aromatic-methyl interactions and helical structure effects in lysozyme.
- Proton nuclear Overhauser effect study of the heme active site structure of chloroperoxidase.
- Data-sieving hydrophobicity plots.
- A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin.
- NMR of proteins and nucleic acids
Cited by
- Structural studies on large fragments of G protein coupled receptors.
- Heteronuclear NMR studies of human serum apolipoprotein A‐I
- The C-terminal domain of alpha-spectrin is structurally related to calmodulin.
- Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel.
- Mapping the functional surface of insulin by design: structure and function of a novel A-chain analogue.
- Differential involvement of disulfide bridges on the folding of a scorpion toxin.
- Solution structure of αtα, a helical hairpin peptide of de novo design
- A cytoplasmic peptide of the neurotrophin receptor p75NTR: induction of apoptosis and NMR determined helical conformation
- The Solution Structure and Dynamics of the Pleckstrin Homology Domain of G Protein-coupled Receptor Kinase 2 (β-Adrenergic Receptor Kinase 1)
- How a protein prepares for B12 binding: structure and dynamics of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum.
- Structure of Two Fragments of the Third Cytoplasmic Loop of the Rat Angiotensin II AT1A Receptor
- Structural features of a peptide corresponding to human κ-casein residues 84–101 by 1H-nuclear magnetic resonance spectroscopy
- Structural Studies on Phospholamban and Implications for Regulation of the Ca2+‐ATPase
- Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.
- Sequence dependence of β‐hairpin structure: Comparison of a salt bridge and an aromatic interaction
- Synthetic peptides as probes for conformational preferences of domains of membrane receptors
- NMR structures and orientation of the fourth transmembrane domain of the rat divalent metal transporter (DMT1) with G185D mutation in SDS micelles
- Letter to the Editor: Backbone resonance assignment of protease from Mason-Pfizer monkey virus
- Nearest-neighbor effects on backbone alpha and beta carbon chemical shifts in proteins
- Three-dimensional structure of Phyllomedusin, a NK1 receptor agonist bound to dodecylphosphocholine micelles.
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