Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins.
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Summary
Two-dimensional correlated spectroscopy (COSY) is used for measurements of proton-proton spin-spin coupling constants in protein 1H NMR spectra and provides greatly improved spectral resolution.
- Type
- article
- Published
- 1983-06-29
- Cited by
- 2,669
- References
- 21
- OpenAlex
- https://openalex.org/W2093700493
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:2513918
Keywords
Coupling constant, Chemistry, Spin (aerodynamics), Spectroscopy, Proton
References
- NMR in biological research: Peptides and proteins
- Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor homologue K from Dendroaspis polylepis polylepis. Two-dimensional nuclear magnetic resonance at 360 and 500 MHz.
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles.
- Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor.
- Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation
- Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
- Truncated driven nuclear overhauser effect (TOE). A new technique for studies of selective 1H1H overhauser effects in the presence of spin diffusion
- A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants☆
- The use of cross-sections and of projections in two-dimensional NMR spectroscopy
- Analysis of the 1H‐NMR spectra of ferrichrome peptides. II. The amide resonances
- Two‐dimensional spectroscopy. Application to nuclear magnetic resonance
- Structural interpretation of vicinal proton-proton coupling constants 3JH alpha H beta in the basic pancreatic trypsin inhibitor measured by two-dimensional J-resolved NMR spectroscopy.
- Experimental techniques of two-dimensional correlated spectroscopy
- Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance.
- Use of nuclear Overhauser effect in the study of peptides and proteins.
- Spin—spin coupling and the conformational states of peptide systems
- Homonuclear broad band decoupling and two-dimensional J-resolved NMR spectroscopy
- Investigation of complex networks of spin-spin coupling by two-dimensional NMR
- Sequential individual resonance assignments in the 1H nuclear-magnetic-resonance spectrum of cardiotoxin VII2 from Naja mossambica mossambica.
- Analysis of the 1H‐NMR spectra of ferrichrome peptides. I. The non‐amide protons
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- An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
- Comparison of the solution conformations of human [Zn7]-metallothionein-2 and [Cd7]-metallothionein-2 using nuclear magnetic resonance spectroscopy.
- Minor-groove recognition of the self-complementary duplex d(CGCGAATTCGCG)2 by Hoechst 33258: a high-field NMR study.
- NMR structural refinement of a tandem G.A mismatched decamer d(CCAAGATTGG)2 via the hybrid matrix procedure.
- Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution.
- Structural characterization of the interactions between calmodulin and skeletal muscle myosin light chain kinase: effect of peptide (576-594)G binding on the Ca2+-binding domains.
- Two-dimensional NMR studies of Kazal proteinase inhibitors. 1. Sequence-specific assignments and secondary structure of turkey ovomucoid third domain.
- Application of a T2,‐filtered COSY experiment to identify the origin of slowly relaxing species in normal and malignant tissue
- Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles.
- Structural definition of arabinomannans from Mycobacterium bovis BCG
- 4-Epidihydrocochlioquinone B and 14-Epicochlioqumone B, Antibiotics from Fermentations of the Ascomycete Neobulgaria pura: Structure Elucidation and Effects on Platelet Aggregation
- 1H and 15N nuclear magnetic resonance assignments, secondary structure in solution, and solvent exchange properties of azurin from Alcaligenes denitrificans.
- Solution structure of P05-NH2, a scorpion toxin analog with high affinity for the apamin-sensitive potassium channel.
- Conformation of polyene antibiotic, filipin III: CD and 1H NMR studies.
- Solution conformation of a cyclophilin-bound proline isomerase substrate.
- NMRPipe: A multidimensional spectral processing system based on UNIX pipes
- Two-, three-, and four-dimensional nuclear magnetic resonance spectroscopy of protein pharmaceuticals.
- Nmr Structural Characterization of Oligo-N-Substituted Glycine Lead Compounds from a Combinatorial Library
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