X-ray Structures of the Proprotein ConvertaseFurin Bound with Substrate Analogue Inhibitors Reveal Substrate SpecificityDeterminants beyond the S4Pocket
X-ray Structures of the Proprotein ConvertaseFurin Bound with Substrate Analogue Inhibitors Reveal Substrate SpecificityDeterminants beyond the S4Pocket
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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08-30-2011 04:52 PM
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
NMR spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.
Protein Sci. 2011 Jun 1;
Authors: Koculi E, Horst R, Horwich AL, Wüthrich K
NMR observation of the uniformly (2) H,(15) N-labeled stringent 33 kDa substrate protein rhodanese in a productive complex with the uniformly (14) N-labeled 400 kDa single-ring version of the E. coli chaperonin GroEL, SR1,...
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06-03-2011 10:20 AM
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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02-10-2011 03:51 PM
[NMR paper] Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Related Articles Direct NMR observation of a substrate protein bound to the chaperonin GroEL.
Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12748-53
Authors: Horst R, Bertelsen EB, Fiaux J, Wider G, Horwich AL, Wüthrich K
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized. In contrast, very little is known about the nonnative states of the substrate polypeptide acted on by the...
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12-01-2010 06:56 PM
[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p
Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR.
J Am Chem Soc. 2005 Jan 19;127(2):567-75
Authors: Tepper AW, Bubacco L, Canters GW
The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...
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11-24-2010 11:14 PM
[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Biochemistry. 1994 May 31;33(21):6631-41
Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN
The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
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08-22-2010 03:33 AM
[NMR paper] Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic a
Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Related Articles Proton NMR investigation of substrate-bound heme oxygenase: evidence for electronic and steric contributions to stereoselective heme cleavage.
Biochemistry. 1994 May 31;33(21):6631-41
Authors: Hernández G, Wilks A, Paolesse R, Smith KM, Ortiz de Montellano PR, La Mar GN
The substrate-bound form of the enzyme heme oxygenase (HO), which catalyzed the stereospecific alpha-meso bridge...
X-ray Structures of the Proprotein ConvertaseFurin Bound with Substrate Analogue Inhibitors Reveal Substrate SpecificityDeterminants beyond the S4Pocket
Linear Mode
