nmr spectroscopic data processing software (Bruker Corporation)
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Bruker Corporation
nmr spectroscopic data processing software
Nmr Spectroscopic Data Processing Software, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nmr+spectroscopic+data+processing+software/nmr+software/pmc11855265__CHEM___31___e202403960___s001-23-1-7
Average 90 stars, based on 1 article reviews
Nmr Spectroscopic Data Processing Software, supplied by Bruker Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/nmr+spectroscopic+data+processing+software/nmr+software/pmc11855265__CHEM___31___e202403960___s001-23-1-7
Average 90 stars, based on 1 article reviews
nmr spectroscopic data processing software - by Bioz Stars,
2026-09
90/100 stars
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Nuclear Magnetic Resonance:Article Title: Detecting Small Structural Changes in Metalloproteins by the Use of NMR Pseudocontact Shifts Article Snippet: The potential use of pseudocontact shifts (PCS) for detecting small structural changes that may occur in a protein in aqueous solution as a function of temperature is demonstrated on lanthanide-substituted calbindin D9k.. The protein is a dicalcium protein in which one of the calcium ions can be selectively substituted by lanthanides.. The solution structure of the protein had been previously solved at 300 K. New sets of PCS that could readily be obtained at 280 and 310 K from 1H-15N HSQC experiments, together with the other constraints used for the 300 K structure, were used to recalculate the solution structure at the new temperatures, since the new solution structures are consistent with different sets of PCS constraints and a single NOE/dihedral angle set of constraints. Article Title: Easily Accessible and Solution‐Stable Ni(0) Precatalysts for High‐Throughput Experimentation Article Snippet: .. All Software:Article Title: Detecting Small Structural Changes in Metalloproteins by the Use of NMR Pseudocontact Shifts Article Snippet: The potential use of pseudocontact shifts (PCS) for detecting small structural changes that may occur in a protein in aqueous solution as a function of temperature is demonstrated on lanthanide-substituted calbindin D9k.. The protein is a dicalcium protein in which one of the calcium ions can be selectively substituted by lanthanides.. The solution structure of the protein had been previously solved at 300 K. New sets of PCS that could readily be obtained at 280 and 310 K from 1H-15N HSQC experiments, together with the other constraints used for the 300 K structure, were used to recalculate the solution structure at the new temperatures, since the new solution structures are consistent with different sets of PCS constraints and a single NOE/dihedral angle set of constraints. |