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Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures - ACS Publications
Mar 09, 2025 - 9:12 AM - by nmrlearner
nmrlearner's Avatar Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures - ACS Publications

Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures ACS Publications Read here
0 Replies | 32 Views
NMR structures of two designed proteins with high sequence identity but different fold and function - pnas.org
Mar 09, 2025 - 9:12 AM - by nmrlearner
nmrlearner's Avatar NMR structures of two designed proteins with high sequence identity but different fold and function - pnas.org

NMR structures of two designed proteins with high sequence identity but different fold and function pnas.org Read here
0 Replies | 36 Views
Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy - pnas.org
Mar 08, 2025 - 1:15 AM - by nmrlearner
nmrlearner's Avatar Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy - pnas.org

Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy pnas.org Read here
0 Replies | 38 Views
[NMR paper] Exploring the biochemical landscape of bacterial medium with pyruvate as the exclusive carbon source for NMR studies
Mar 07, 2025 - 4:49 AM - by nmrlearner
nmrlearner's Avatar Exploring the biochemical landscape of bacterial medium with pyruvate as the exclusive carbon source for NMR studies

The use of Escherichia coli for recombinant protein production is a cornerstone in structural biology, particularly for nuclear magnetic resonance (NMR) spectroscopy studies. Understanding the metabolic behavior of E. coli under different carbon sources is critical for optimizing isotope labeling strategies, which are essential for protein structure determination by NMR. Recent advancements, such as mixed pyruvate labeling, have enabled improved backbone resonance assignment in large proteins,...

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0 Replies | 183 Views
Exploring the biochemical landscape of bacterial medium with pyruvate as the exclusive carbon source for NMR studies
Mar 06, 2025 - 4:47 PM - by nmrlearner
nmrlearner's Avatar Exploring the biochemical landscape of bacterial medium with pyruvate as the exclusive carbon source for NMR studies

The use of Escherichia coli for recombinant protein production is a cornerstone in structural biology, particularly for nuclear magnetic resonance (NMR) spectroscopy studies. Understanding the metabolic behavior of E. coli under different carbon sources is critical for optimizing isotope labeling strategies, which are essential for protein structure determination by NMR. Recent advancements, such as mixed pyruvate labeling, have enabled improved backbone resonance assignment in large proteins, making selective isotopic labeling strategies more important than ever for NMR studies. In this study, we aimed to investigate the metabolic adaptations of E. coli when grown on pyruvate as the sole carbon source, a common condition used to achieve selective labeling for NMR spectroscopy. Using NMR-based metabolomics, we tracked key metabolic shifts throughout the culture process to better understand how pyruvate metabolism affects protein production and isotopic labeling. Our results reveal that pyruvate is rapidly depleted before IPTG induction, while acetate and lactate accumulate due to overflow metabolism. These byproducts persist after induction, indicating that pyruvate is diverted into waste pathways, which limits its efficient use in isotope incorporation. This metabolic inefficiency presents a challenge for isotopic labeling protocols that rely on pyruvate as a carbon source for NMR studies. Our results highlight the need to fine-tune pyruvate supplementation to improve metabolic efficiency and isotopic labeling, making this study directly relevant to optimizing protocols for NMR studies involving protein structure determination. These insights provide valuable guidance for enhancing the quality and yield of isotopically labeled proteins in NMR... [Read More]
0 Replies | 74 Views
Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR - pnas.org
Mar 06, 2025 - 4:47 PM - by nmrlearner
nmrlearner's Avatar Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR - pnas.org

Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR pnas.org Read here
0 Replies | 36 Views
Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2 - Wiley Online Library
Mar 06, 2025 - 4:47 PM - by nmrlearner
nmrlearner's Avatar Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2 - Wiley Online Library

Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2 Wiley Online Library Read here
0 Replies | 41 Views
Xplor-NIH: Better parameters and protocols for NMR protein structure determination - Wiley Online Library
Mar 06, 2025 - 4:34 AM - by nmrlearner
nmrlearner's Avatar Xplor-NIH: Better parameters and protocols for NMR protein structure determination - Wiley Online Library

Xplor-NIH: Better parameters and protocols for NMR protein structure determination Wiley Online Library Read here
0 Replies | 41 Views
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