RNA Hairpin Folding in the Crowded Cell

Mimi Gao1, David Gnutt1, Axel Orban2

  • 1Physical Chemistry II, Ruhr-Universität Bochum, Universitätsstr. 150, 44801, Bochum, Germany.

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.

Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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 Folding01:25

Protein Folding

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...
12.5K
Protein Folding01:22

Protein Folding

Overview
130.4K
Protein Folding01:22

Protein Folding

36.4K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
20.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.5K