Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy

1990 ◽  
Vol 112 (24) ◽  
pp. 9020-9022 ◽  
Author(s):  
Mitsuhiko Ikura ◽  
Ad Bax ◽  
G. Marius Clore ◽  
Angela M. Gronenborn
Keyword(s):  
Nmr Spectroscopy ◽  
Three Dimensional ◽  
Amide Proton ◽  
Proton Resonances ◽  
Nuclear Overhauser ◽  
Nuclear Overhauser Effects

scholarly journals Characterization of the structure and redox behaviour of cytochrome c3 from Desulfovibrio baculatus by 1H-nuclear-magnetic-resonance spectroscopy

1993 ◽  
Vol 294 (3) ◽  
pp. 899-908 ◽  
Author(s):  
I B Coutinho ◽  
D L Turner ◽  
J LeGall ◽  
A V Xavier
Keyword(s):  
Chemical Shifts ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Resonance Spectroscopy ◽  
Cytochrome C3 ◽  
X Ray ◽  
1H Nuclear Magnetic Resonance ◽  
Proton Resonances ◽  
Nuclear Overhauser

Complete assignment of the aromatic and haem proton resonances in the cytochromes c3 isolated from Desulfovibrio baculatus strains (Norway 4, DSM 1741) and (DSM 1743) was achieved using one- and two-dimensional 1H n.m.r. Nuclear Overhauser enhancements observed between haem and aromatic resonances and between resonances due to different haems, together with the ring-current contributions to the chemical shifts of haem resonances, support the argument that the haem core architecture is conserved in the various cytochromes c3, and that the X-ray structure of the D. baculatus cytochrome c3 is erroneous. The relative orientation of the haems for both cytochromes was determined directly from n.m.r. data. The n.m.r. structures have a resolution of approximately 0.25 nm and are found to be in close agreement with the X-ray structure from D. vulgaris cytochrome c3. The proton assignments were used to relate the highest potential to a specific haem in the three-dimensional structure by monitoring the chemical-shift variation of several haem resonances throughout redox titrations followed by 1H n.m.r. The haem with highest redox potential is not the same as that in other cytochromes c3.

N.M.R. studies of myelin basic protein. V. 1H N.M.R. of the peptides encephalitogenic in guinea pig

1981 ◽  
Vol 34 (7) ◽  
pp. 1373 ◽  
Author(s):  
SA Margetson ◽  
WJ Moore ◽  
WA Gibbons
Keyword(s):  
Myelin Basic Protein ◽  
Ring Current ◽  
Basic Protein ◽  
Chemical Shifts ◽  
C Terminus ◽  
Proton Resonances ◽  
Nuclear Overhauser ◽  
Nuclear Overhauser Effects ◽  
Peptide Data ◽  
Made In

The 1H n.m.r. spectra of the following peptides have been investigated: (1) the encephalitogenic H-Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Lys-OH comprising residues 114-122 of bovine myelin basic protein, (2) the corresponding -Arg-OH peptide of human basic protein, (3) the inactive peptide in which D-Ala5 replaces L-Ala5. Measurements were made in D2O solutions at 270 and 600 MHz over a range of temperatures, concentrations and pH. All the proton resonances have been assigned by comparisons with other peptide data, titration shifts, selective decoupling and nuclear Overhauser effects, and data on the (α,α- 2H2)Gly7 nonapeptide. Ring current shifts and their temperature dependence indicated that there is preferential stacking of the Phe and Trp rings, and also interactions between these rings and the Gln and Lys residues near the C-terminus of the peptide. These data suggest a reverse turn at the Gly4-Ala5 residues, a conformation that would be consistent with results from energy calculations and biological activity. The n.m.r. spectra of the L-Ala and D-Ala peptides differed in the temperature coefficients of certain chemical shifts, including particularly those subject to ring current effects. Data in dimethyl sulfoxide were limited by effects of aggregation, but definite conformation differences compared to aqueous solutions were indicated.

scholarly journals Interactions of integrin GPIIb/IIIa-derived peptides with fibrinogen investigated by NMR spectroscopy

1996 ◽  
Vol 315 (1) ◽  
pp. 161-170 ◽  
Author(s):  
Letitia J. YAO ◽  
Kevin H. MAYO
Keyword(s):  
Nmr Spectroscopy ◽  
Bound States ◽  
Distance Geometry ◽  
Integrin Receptor ◽  
Hydrophobic Residues ◽  
Fibrinogen Binding ◽  
Nuclear Overhauser ◽  
Nuclear Overhauser Effects ◽  
Exchange Regime ◽  
Positively Charged

Three peptides derived from platelet integrin receptor glycoprotein αIIbβ3 (GPIIb/IIIa) have been identified recently as fibrinogen-binding sequences: GPIIb 300–314 and 656–667 and GPIIIa 211–223. NMR spectroscopy has been used here to investigate the interactions of these peptides with parent fibrinogen. Based on resonance broadening and chemical-shift changes of peptides in the presence and absence of fibrinogen, interactions in the fast ligand-exchange regime are apparent and interfacial residues can be proposed. Positively charged arginines and histidines, along with several hydrophobic residues, are implicated as being crucial to the binding process. Transferred nuclear Overhauser effects and distance geometry calculations allow discussion of probable conformations in peptide-‘bound’ states. These identifications are consistent with other biological/ chemical data and provide the basis for further studies aimed at understanding fibrinogen-mediated platelet aggregation on the molecular level.

scholarly journals 2P-022 Investigating protein three-dimensional structures inside living cells by in-cell NMR spectroscopy(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S78
Author(s):  
Junpei Hamatsu ◽  
Daisuke Sakakibara ◽  
Atsuko Sasaki ◽  
Teppei Ikeya ◽  
Masaki Mishima ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Annual Meeting ◽  
Three Dimensional ◽  
Living Cells ◽  
Biophysical Society

scholarly journals NMR solution conformation of heparin-derived tetrasaccharide

1996 ◽  
Vol 318 (1) ◽  
pp. 93-102 ◽  
Author(s):  
Dmitri MIKHAILOV ◽  
Kevin H. MAYO ◽  
Ioncho R. VLAHOV ◽  
Toshihiko TOIDA ◽  
Azra PERVIN ◽  
...  
Keyword(s):  
Chair Conformation ◽  
Coupling Constants ◽  
Solution Conformation ◽  
1H And 13C Nmr ◽  
Small Deviations ◽  
J Coupling Constants ◽  
Nuclear Overhauser ◽  
Nuclear Overhauser Effects ◽  
Dynamics Simulations ◽  
Ring Conformations

The solution conformation of the homogeneous, heparin-derived tetrasaccharide ΔUA2S(1 → 4)-α-d-GlcNpS6S(1 → 4)-α-l-IdoAp2S(1 → 4)-α-d-GlcNpS6S (residues A, B, C and D respectively, where IdoA is iduronic acid) has been investigated by using 1H- and 13C-NMR. Ring conformations have been defined by J-coupling constants and inter-proton nuclear Overhauser effects (NOEs), and the orientation of one ring with respect to the other has been defined by inter-ring NOEs. NOE-based conformational modelling has been done by using the iterative relaxation matrix approach (IRMA), restrained molecular dynamics simulations and energy minimization to refine structures and to distinguish between minor structural differences and equilibria between various ring forms. Both glucosamine residues B and D are in the 4C1 chair conformation. The 6-O-sulphate group is oriented in the gauche–trans configuration in the D ring, whereas in the B ring the gauche–gauche rotomer predominates. Uronate (A) and iduronate (C) residues are mostly represented by 1H2 and 2S0 twisted boat forms, respectively, with small deviations in expected coupling constants and NOEs suggesting minor contributions from other A and C ring conformations.

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