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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

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Published on: February 12, 2022

Current Solution NMR Techniques for Structure-Function Studies of Proteins and RNA Molecules.

John L Markley¹

¹Biochemistry Department, University of Wisconsin-Madison, Madison, WI, USA. jmarkley@wisc.edu.

Advances in Experimental Medicine and Biology

|January 9, 2019

Summary

Nuclear Magnetic Resonance (NMR) spectroscopy allows studying dynamic biomolecules in solution at atomic resolution. This review covers NMR methods for structure-function analysis, including labeling, data collection, and analysis.

Keywords:

Data deposition Dynamics Functional studies NMR data collection strategies NMR observables NMR software packages Spectral assignment Stable isotope labeling Structural restraints Validation of NMR results

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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation

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Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

Biochemistry and structural biology
Biophysical chemistry

Background:

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for investigating biological macromolecules.
Studying molecules in solution under physiological conditions is crucial for understanding their dynamic functions.

Purpose of the Study:

To review current technologies for structure-function investigations of biological macromolecules using NMR spectroscopy.
To highlight the advantages of NMR for studying dynamic biomolecules at atomic resolution.

Main Methods:

Stable isotope labeling strategies for enhanced NMR signals.
NMR data collection methodologies tailored for biomolecules.
Data analysis procedures for deriving structure-function insights.

Main Results:

NMR enables atomic-resolution studies of biomolecules in near physiological conditions.
Hybrid methods combining NMR with other techniques are facilitated.
Key aspects of NMR data processing and interpretation are discussed.

Conclusions:

NMR spectroscopy is a vital tool for understanding biomolecular structure and function in a dynamic context.
Standardized approaches to NMR data collection, analysis, and deposition are important for reproducibility.