[NMR paper] NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evi
NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
Related Articles NMR studies of 4-19F-phenylalanine-labeled intestinal fatty acid binding protein: evidence for conformational heterogeneity in the native state.
Biochemistry. 2005 Feb 22;44(7):2369-77
Authors: Li H, Frieden C
(19)F-Nuclear magnetic resonance (NMR) studies have been carried out after incorporation of 4-(19)F-phenylalanine into the intestinal fatty acid binding protein (IFABP), a...
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11-24-2010 11:14 PM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Biochemistry. 1994 Apr 12;33(14):4093-100
Authors: Cheng JW, Lepre CA, Moore JM
Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
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08-22-2010 03:33 AM
[NMR paper] NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
Related Articles NMR studies of the FK506 binding protein bound to a spin-labeled ascomycin analog.
J Magn Reson B. 1994 May;104(1):77-80
Authors: Yu L, Meadows RP, Wagner R, Fesik SW
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08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand bi
15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition.
Biochemistry. 1994 Apr 12;33(14):4093-100
Authors: Cheng JW, Lepre CA, Moore JM
Backbone dynamics of the ligand- (FK506-) bound protein FKBP-12 (107 amino acids) have been examined using 15N relaxation data derived from inverse-detected two-dimensional...
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08-22-2010 03:33 AM
[NMR paper] 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the unc
15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Related Articles 15N NMR relaxation studies of the FK506 binding protein: backbone dynamics of the uncomplexed receptor.
Biochemistry. 1993 Sep 7;32(35):9000-10
Authors: Cheng JW, Lepre CA, Chambers SP, Fulghum JR, Thomson JA, Moore JM
Backbone dynamics of the major tacrolimus (FK506) binding protein (FKBP-12, 107 amino acids) have been studied using 15N relaxation data derived from proton-detected two-dimensional 1H-15N NMR spectroscopy....
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08-22-2010 03:01 AM
[NMR paper] Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppres
Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex.
Related Articles Heteronuclear 3D NMR studies of water bound to an FK506 binding protein/immunosuppressant complex.
Biochemistry. 1993 Mar 16;32(10):2473-80
Authors: Xu RX, Meadows RP, Fesik SW
From a series of 15N-resolved 3D ROESY-HMQC and 13C-resolved 3D NOESY-HMQC spectra of the FK506 binding protein (FKBP)/ascomycin complex in H2O, the locations of three tightly bound water molecules were identified. These waters are all buried within the...
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08-21-2010 11:53 PM
[NMR paper] Three-dimensional structure of the FK506 binding protein/ascomycin complex in solutio
Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
Related Articles Three-dimensional structure of the FK506 binding protein/ascomycin complex in solution by heteronuclear three- and four-dimensional NMR.
Biochemistry. 1993 Jan 26;32(3):754-65
Authors: Meadows RP, Nettesheim DG, Xu RX, Olejniczak ET, Petros AM, Holzman TF, Severin J, Gubbins E, Smith H, Fesik SW
A high-resolution three-dimensional solution structure of the FKBP/ascomycin complex has been...
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[NMR paper] NMR studies of an FK-506 analog, [U-13C]ascomycin, bound to FK-506-binding protein.
NMR studies of an FK-506 analog, ascomycin, bound to FK-506-binding protein.
Related Articles NMR studies of an FK-506 analog, ascomycin, bound to FK-506-binding protein.
J Med Chem. 1992 Jun 26;35(13):2467-73
Authors: Petros AM, Gemmecker G, Neri P, Olejniczak ET, Nettesheim D, Xu RX, Gubbins EG, Smith H, Fesik SW
Multidimensional, heteronuclear NMR methods were used to determine the complete 1H and 13C resonance assignments for ascomycin bound to recombinant FKBP, including stereospecific assignment of all 22 methylene protons. The...