Protein Nmr Studies
Protein Nmr Studies - Related Videos
04:33
Quantitative In-Cell Hydrogen NMR Spectroscopy to Monitor Protein-Ligand Interactions
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2025
In this video, we demonstrate the in-cell nuclear magnetic resonance spectroscopy technique to study protein-ligand interactions between unlabeled overexpressed proteins and small molecules. The successful ligand-protein interaction is confirmed visually by the appearance of an additional set of peaks in the spectral region of interest that gradually replaces the original peaks.
10:10
Transport Properties of Ibuprofen Encapsulated in Cyclodextrin Nanosponge Hydrogels: A Proton HR-MAS NMR Spectroscopy Study
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Cited by 11 •
2016
The motion regimes of ibuprofen encapsulated in β-cyclodextrin nanosponges polymer network are investigated using pulsed-field-gradient spin-echo (PGSE) NMR technique. Synthesis, purification, drug loading, implementation of the NMR pulse sequence and data analysis to work out the mean square displacement of the drug at several observation times are described in detail.
13:59
Methods to Identify the NMR Resonances of the 13C-Dimethyl N-terminal Amine on Reductively Methylated Proteins
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Cited by 4 •
2013
Two methods for assigning the α- and ε-dimethylamine nuclear magnetic resonance signals of a reductively 13C-methylated N-terminal lysine are described. One method utilizes the pH-induced selectivity of the reductive methylation reaction, and the other uses aminopeptidase to selectively remove the N-terminal lysine.
06:05
Nuclear Magnetic Resonance to Study Atomic Level Protein-Protein Interactions
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2025
This video describes the nuclear magnetic resonance spectroscopy technique to study protein-protein interactions between 15N-labeled wild-type and mutant envoplakin proteins and the unlabeled vimentin protein. The successful interaction between wild-type envoplakin and vimentin leads to extensive line broadening and peak disappearance in the NMR spectra, whereas the absence of an interaction between the mutated envoplakin and vimentin results in well-resolved peaks in the NMR spectra.
11:44
Spin Saturation Transfer Difference NMR (SSTD NMR): A New Tool to Obtain Kinetic Parameters of Chemical Exchange Processes
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Cited by 4 •
2016
A detailed protocol describing the SSTD NMR method is presented here to help new users apply this new method to obtain the kinetic parameters of their own systems undergoing chemical exchange.
FAQs
Chemical shifts provide environment-dependent frequencies that help map a protein's local chemical setting. When interpreted alongside scalar couplings, they contribute information about atomic connectivity, while changes in shifts can indicate altered conformations or molecular interactions. This makes them useful for following structural responses during chemical or biological studies.
Each measurement contributes a different constraint. Scalar couplings report through-bond relationships, nuclear Overhauser effects indicate spatial proximity, and relaxation measurements describe motion. Combining these signals is more informative than treating any one observable as a complete structural picture. The resulting pattern helps connect molecular arrangement with protein dynamics.
Protein NMR studies can be especially informative when researchers need to examine a protein in solution rather than rely on crystallization. This solution-based perspective supports observation of dynamics, conformational changes, and interactions under the measured conditions. It therefore complements structural approaches focused on obtaining a crystal, particularly for questions involving motion or changing states.
Binding can alter the chemical environment of nuclei near an interaction site, producing changes in measured NMR signals. Interpreting those changes helps locate binding sites and detect associated conformational adjustments. In chemistry, this provides a way to examine protein-ligand interactions and connect molecular recognition with changes that may influence protein function.
In chemistry, these studies support mechanistic investigations, biomolecular design, and the development of compounds intended to modulate protein function. Their value extends beyond describing a static structure: measurements can connect interactions, conformational changes, and dynamics with the behavior of a molecular system. This makes the approach relevant to both fundamental and applied research.
Researchers can use structural and dynamic information to examine how proteins move through folding pathways rather than considering only a final conformation. NMR observables provide complementary evidence about local environments, connectivity, proximity, and motion. Together, these signals can help relate changes during folding to underlying molecular behavior in solution.