Stereospecific assignment of β-methylene protons in larger proteins using 3D15N-separated Hartmann-Hahn and13C-separated rotating frame Overhauser spectroscopy
Explore this paper's citation graph
Summary
It is demonstrated that reliable information on the intraresidue CxH−CβH distances, free of systematic errors arising from spin diffusion, can be obtained from a 3D13C-separated1H−1H rotating frame Overhauser effect 1H−13C multiple quantum coherence (ROESY-HMQC) spectrum.
- Type
- article
- Published
- 1991-05-01
- Cited by
- 84
- References
- 47
- OpenAlex
- https://openalex.org/W1668718
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:4951670
Keywords
Iconography, Art, Art history
References
- Stereochemistry of binding of the tetrapeptide acetyl-Pro-Ala-Pro-Tyr-NH2 to porcine pancreatic elastase. Combined use of two-dimensional transferred nuclear Overhauser enhancement measurements, restrained molecular dynamics, X-ray crystallography and molecular modelling.
- Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.
- The influence of stereospecific assignments on the determination of three‐dimensional structures of proteins by nuclear magnetic resonance spectroscopy
- Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes.
- Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing.
- Assignment of complex proton NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
- Analysis of the relationship between side-chain conformation and secondary structure in globular proteins.
- Side chain conformations of oxytocin and vasopressin studied by NMR observation of isotopic isomers
- A heteronuclear three-dimensional NMR experiment for measurements of small heteronuclear coupling constants in biological macromolecules
- Automated stereospecific 1H NMR assignments and their impact on the precision of protein structure determinations in solution
- Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame
- Multiple quantum filters for elucidating NMR coupling networks
- Broadband homonuclear cross polarization in 2D N.M.R. using DIPSI-2
- P.E.COSY, a simple alternative to E.COSY
- A comparison of the ROESY and NOESY experiments for large molecules, with application to nucleic acids
- Direct identification of relayed nuclear overhauser effects
- Sensitivity enhanced detection of weak nuclei using heteronuclear multiple quantum coherence
- Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy.
- Spin—spin coupling and the conformational states of peptide systems
- Iterative schemes for bilinear operators; application to spin decoupling
Cited by
- Two-, three-, and four-dimensional nuclear magnetic resonance spectroscopy of protein pharmaceuticals.
- Decreased entropy of unfolding increases the temperature of maximum stability : Thermodynamic stability of a thioredoxin from the hyperthermophilic archaeon Methanococcus jannaschii
- Physical Methods to Characterize Pharmaceutical Proteins
- Multidimensional heteronuclear nuclear magnetic resonance of proteins.
- NMR structure of the Tn916 integrase–DNA complex
- A novel loop-loop recognition motif in the yeast ribosomal protein L30 autoregulatory RNA complex
- One HAT size fits all?
- Experimental NMR techniques for studies of biopolymers
- Estudos termodinâmicos e estruturais da interação cabeça-cauda da , alpha-tropomiosina muscular
- Determination of HN,Hα and HN,C′ coupling constants in 13C, 15N-labeled proteins
- Use of nuclear magnetic resonance spectroscopy to study structure-function of bromodomains.
- The Mu repressor–DNA complex contains an immobilized 'wing' within the minor groove
- Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins.
- Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal
- The structure in solution of the b domain of protein disulfide isomerase*
- Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type.
- The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.
- High‐resolution solution structure of Bacillus subtilis IIAglc
- Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0.
- Isotope labeling in solution protein assignment and structural analysis
Related papers
No related papers recorded.