Related Experiment Video
Updated: Mar 26, 2026

06:59
Nanomanipulation of Single RNA Molecules by Optical Tweezers
Published on: August 20, 2014
15.6K
RNA Hairpin Folding in the Crowded Cell
Mimi Gao1, David Gnutt1, Axel Orban2
1Physical Chemistry II, Ruhr-Universität Bochum, Universitätsstr. 150, 44801, Bochum, Germany.
Angewandte Chemie (International Ed. in English)
|February 3, 2016
Summary
This study measured ribonucleic acid (RNA) hairpin structure stability within live cells, finding it similar to in vitro conditions. Cellular environments cause localized effects, but overall RNA folding stability is only marginally modulated.
Area of Science:
- Molecular Biology
- Biophysics
- Cell Biology
Background:
- Accurate ribonucleic acid (RNA) structure is vital for cellular functions.
- Previous RNA folding studies were limited to in vitro conditions, lacking cellular validation.
Purpose of the Study:
- To directly measure the folding stability of a hairpin-structured RNA within live mammalian cells.
- To compare intracellular RNA stability with in vitro conditions and assess the impact of crowding agents.
Main Methods:
- Directly resolving hairpin-structured RNA folding stability in live mammalian cells.
- Comparing stability in dilute physiological buffer, within cells, and with artificial crowding agents in vitro.
Main Results:
- Intracellular RNA hairpin stability is comparable to dilute physiological buffer.
- In vitro crowding agents, except high-molecular-weight PEG, destabilized the RNA structure.
- Significant variability in RNA stability was observed within cell populations and subcellular regions (cytosol and nucleus).
Conclusions:
- Intracellular RNA folding stability is only marginally modulated on average compared to diluted buffer.
- Localized stabilizing and destabilizing effects exist within cellular compartments.
- Cellular environment plays a complex role in RNA structural stability.
Related Concept Videos
Single-Strand DNA Binding Proteins
17.2K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
17.2K
Protein Folding
12.5K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.5K
Protein Folding
130.4K
Overview
130.4K
Protein Folding
36.4K
36.4K
Molecular Chaperones and Protein Folding
20.8K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
20.8K
Molecular Chaperones and Protein Folding
15.5K
15.5K

