Sn-? zeolites prepared using different recipes feature very different catalytic activities for aqueous phase glucose isomerization, suggesting the presence of different active sites. A systematic study of the morphology and atomic-level structure of the materials using DNP NMR spectroscopy in combination with first-principles calculations allows for the discrimination between potential sites and leads to a proposal of specific structural features that are important for high activity. The results indicate that the materials showing the highest activity possess a highly hydrophobic, defect-free zeolite framework. Those materials show so-called closed and associated partially hydrolyzed Sn(IV) sites in the T6 and T5/T7 lattice positions. On the other hand, postsynthetically synthesized Sn-? samples prepared in two steps via dealumination and subsequent solid-state ion exchange from Al-? show significantly lower activity, which is associated with a hydrophilic framework and/or a lower accessibility and different lattice position of the Sn sites in the zeolite crystal. Further, we provide a method to distinguish between different Sn sites on the basis of NMR cartography using chemical shift and chemical shift anisotropy as readily measurable parameters. This cartography allows identifying not only the nature of the active sites (closed, defect-open, and hydrolyzed-open) but also their position within the BEA framework.
[NMR paper] NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
Related Articles NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity.
Biochemistry. 2016 May 10;
Authors: Byeon IL, Byeon CH, Wu T, Mitra M, Singer D, Levin JG, Gronenborn AM
Abstract
Human APOBEC3B (A3B) is a member of the APOBEC3 (A3) family of cytidine deaminases, which function as DNA mutators and restrict viral pathogens and endogenous...
[NMR paper] Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
Amino Acids. 2013 Mar;44(3):821-33
Authors: Su Y, Li S, Hong M
Abstract
Many membrane-active peptides, such as cationic cell-penetrating peptides (CPPs) and antimicrobial peptides...
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[NMR paper] NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
Related Articles NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.
Proc Natl Acad Sci U S A. 2013 Jul 18;
Authors: Sekhar A, Kay LE
Abstract
The importance of dynamics to biomolecular function is becoming increasingly clear. A description of the structure-function relationship must, therefore, include the role of motion, requiring a shift in paradigm from...
[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote
Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.
Peptides. 2002 Dec;23(12):2127-41
Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S
The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the...
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[NMR paper] HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structu
HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations.
Related Articles HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations.
J Magn Reson. 2000 Nov;147(1):138-46
Authors: García de la Torre J, Huertas ML, Carrasco B
The heteronuclear NMR relaxation of globular proteins depends on the anisotropic rotational diffusion tensor. Using our previous developments for prediction of hydrodynamic properties of arbitrarily...
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[NMR paper] Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spec
Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Related Articles Catalytic activity of the SH2 domain of human pp60c-src; evidence from NMR, mass spectrometry, site-directed mutagenesis and kinetic studies for an inherent phosphatase activity.
Biochemistry. 1995 Nov 21;34(46):15351-8
Authors: Boerner RJ, Consler TG, Gampe RT, Weigl D, Willard DH, Davis DG, Edison AM, Loganzo F, Kassel DB, Xu RX
During solution...
Correlating Synthetic Methods, Morphology, Atomic-Level Structure, and Catalytic Activity of Sn-? Catalysts
Linear Mode
