A view on phosphate ester photochemistry by time-resolved solid state NMR. Intramolecular redox reaction of caged ATP

2008 ◽  
Vol 10 (45) ◽  
pp. 6820 ◽  
Author(s):  
Alexey V. Cherepanov ◽  
Elena V. Doroshenko ◽  
Jörg Matysik ◽  
Simon de Vries ◽  
Huub J. M. De Groot
Keyword(s):  
Solid State ◽  
Redox Reaction ◽  
Solid State Nmr ◽  
Phosphate Ester ◽  
Time Resolved ◽  
Caged Atp

scholarly journals `NMR Crystallization': in-situ NMR techniques for time-resolved monitoring of crystallization processes

2017 ◽  
Vol 73 (3) ◽  
pp. 137-148 ◽  
Author(s):  
Kenneth D. M. Harris ◽  
Colan E. Hughes ◽  
P. Andrew Williams ◽  
Gregory R. Edwards-Gau
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Solid Phase ◽  
Dynamic Properties ◽  
Time Resolved ◽  
Nmr Techniques ◽  
Versatile Technique ◽  
Crystallization From Solution ◽  
In Situ Nmr

Solid-state NMR spectroscopy is a well-established and versatile technique for studying the structural and dynamic properties of solids, and there is considerable potential to exploit the power and versatility of solid-state NMR for in-situ studies of chemical processes. However, a number of technical challenges are associated with adapting this technique for in-situ studies, depending on the process of interest. Recently, an in-situ solid-state NMR strategy for monitoring the evolution of crystallization processes has been developed and has proven to be a promising approach for identifying the sequence of distinct solid forms present as a function of time during crystallization from solution, and for the discovery of new polymorphs. The latest development of this technique, called `CLASSIC' NMR, allows the simultaneous measurement of both liquid-state and solid-state NMR spectra as a function of time, thus yielding complementary information on the evolution of both the liquid phase and the solid phase during crystallization from solution. This article gives an overview of the range of NMR strategies that are currently available for in-situ studies of crystallization processes, with examples of applications that highlight the potential of these strategies to deepen our understanding of crystallization phenomena.

scholarly journals Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly

2019 ◽  
Vol 116 (34) ◽  
pp. 16717-16722 ◽  
Author(s):  
Jaekyun Jeon ◽  
Kent R. Thurber ◽  
Rodolfo Ghirlando ◽  
Wai-Ming Yau ◽  
Robert Tycko
Keyword(s):  
Solid State ◽  
Self Assembly ◽  
Solid State Nmr ◽  
Amyloid Formation ◽  
Initial State ◽  
Final State ◽  
Time Resolved ◽  
Structural Conversion ◽  
Structural Order ◽  
Ph Jump

Common experimental approaches for characterizing structural conversion processes such as protein folding and self-assembly do not report on all aspects of the evolution from an initial state to the final state. Here, we demonstrate an approach that is based on rapid mixing, freeze-trapping, and low-temperature solid-state NMR (ssNMR) with signal enhancements from dynamic nuclear polarization (DNP). Experiments on the folding and tetramerization of the 26-residue peptide melittin following a rapid pH jump show that multiple aspects of molecular structure can be followed with millisecond time resolution, including secondary structure at specific isotopically labeled sites, intramolecular and intermolecular contacts between specific pairs of labeled residues, and overall structural order. DNP-enhanced ssNMR data reveal that conversion of conformationally disordered melittin monomers at low pH to α-helical conformations at neutral pH occurs on nearly the same timescale as formation of antiparallel melittin dimers, about 6 to 9 ms for 0.3 mM melittin at 24 °C in aqueous solution containing 20% (vol/vol) glycerol and 75 mM sodium phosphate. Although stopped-flow fluorescence data suggest that melittin tetramers form quickly after dimerization, ssNMR spectra show that full structural order within melittin tetramers develops more slowly, in ∼60 ms. Time-resolved ssNMR is likely to find many applications to biomolecular structural conversion processes, including early stages of amyloid formation, viral capsid formation, and protein–protein recognition.

scholarly journals Time-Resolved Dehydration-Induced Structural Changes in an Intact Bovine Cortical Bone Revealed by Solid-State NMR Spectroscopy

2009 ◽  
Vol 131 (47) ◽  
pp. 17064-17065 ◽  
Author(s):  
Peizhi Zhu ◽  
Jiadi Xu ◽  
Nadder Sahar ◽  
Michael D. Morris ◽  
David H. Kohn ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Cortical Bone ◽  
Solid State Nmr ◽  
Structural Changes ◽  
Time Resolved ◽  
Solid State Nmr Spectroscopy

Detection of the Covalent Intermediate of UDP-N-Acetylglucosamine Enolpyruvyl Transferase by Solution-State and Time-Resolved Solid-State NMR Spectroscopy

Biochemistry ◽  
1994 ◽  
Vol 33 (50) ◽  
pp. 15071-15079 ◽  
Author(s):  
Cecilia Ramilo ◽  
Richard J. Appleyard ◽  
Christoph Wanke ◽  
Florian Krekel ◽  
Nikolaus Amrhein ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Time Resolved ◽  
Solid State Nmr Spectroscopy ◽  
Solution State ◽  
Covalent Intermediate

Time-Resolved Solid-State NMR Spectroscopy of 5-Enolpyruvylshikimate-3-phosphate Synthase

Biochemistry ◽  
1994 ◽  
Vol 33 (22) ◽  
pp. 6812-6821 ◽  
Author(s):  
Richard J. Appleyard ◽  
Wendy A. Shuttleworth ◽  
Jeremy N. S. Evans
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Time Resolved ◽  
Solid State Nmr Spectroscopy ◽  
Phosphate Synthase
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