Results 11 to 20 of about 208,246 (250)
Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density [PDF]
Journal of Biomolecular NMR, 2010 Protein interactions are important for understanding many molecular mechanisms underlying cellular processes. So far, interfaces between interacting proteins have been characterized by NMR spectroscopy mostly by using chemical shift perturbations and cross-saturation via intermolecular cross-relaxation.
Ferrage, Fabien +3 more
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Molecular Thermodynamics Using Nuclear Magnetic Resonance (NMR) Spectroscopy
Inventions, 2019 Nuclear magnetic resonance (NMR) spectroscopy is perhaps the most widely used technology from the undergraduate teaching labs in organic chemistry to advanced research for the determination of three-dimensional structure as well as dynamics of ...
Viswanathan V. Krishnan
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Exchange-selective excitation pulses for dynamic magnetic resonance. [PDF]
Sci AdvCoherent evolution is punctuated by dynamical processes such as chemical exchange, conformational transformation, or site hopping in many important problems ranging from biomolecular function to ion trap quantum computation.
Lindale JR, Warren WS.
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NMR methods for investigating functionally relevant biomolecular dynamics [PDF]
Magnetic Resonance LettersThe dynamics of biomolecules span across a wide range of timescales, reflecting the complexity of free energy landscapes of biomolecules. Among these, the microsecond-to-millisecond (μs–ms) timescale dynamics are particularly significant, offering ...
Yangzhuoyue Jin +2 more
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, 2004 Nuclear magnetic resonance spectroscopy has continuously been developing ever since its introduction as a structural method in bioscience. Recently established residual dipolar coupling techniques yield information on long-range order in weakly aligned samples as they define the orientation of vectors between nuclei in a common global reference ...
S. Meier
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Non-Averaged Single-Molecule 3D Structures Capture RNA Maturation Intermediates by Individual-Particle Cryo-Electron Tomography [PDF]
Structural DynamicsUnderstanding the structural dynamics of biomolecules at the single-particle level is essential for elucidating molecular functions, folding mechanisms, and conformational transitions that underlie biological processes.
Gang Ren, Jianfang Liu, Meng Zhang
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Using delayed decoupling to attenuate residual signals in editing filters [PDF]
Magnetic Resonance, 2021 Isotope filtering methods are instrumental in biomolecular nuclear magnetic resonance (NMR) studies as they isolate signals of chemical moieties of interest within complex molecular assemblies.
K. A. Marincin +3 more
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Correction of field instabilities in biomolecular solid-state NMR by simultaneous acquisition of a frequency reference [PDF]
Magnetic Resonance, 2022 With the advent of faster magic-angle spinning (MAS) and higher magnetic fields, the resolution of biomolecular solid-state nuclear magnetic resonance (NMR) spectra has been continuously increasing.
V. Římal +8 more
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Protein Surface Interactions—Theoretical and Experimental Studies
Frontiers in Molecular Biosciences, 2021 In this review, we briefly describe a theoretical discussion of protein folding, presenting the relative contribution of the hydrophobic effect versus the stabilization of proteins via direct surface forces that sometimes may be overlooked.
Fabio C. L. Almeida +11 more
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Frontiers in Molecular Biosciences, 2021 The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands the redirection of scientific efforts and criteria to organized research projects.
Nadide Altincekic +178 more
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