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Related Concept Videos

RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
RNA Stability01:53

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations between RNA and DNA underlie the differences in their stability and longevity. Because DNA is double-stranded, it is inherently more stable. The single-stranded structure of RNA is less stable but also more flexible and can form weak internal bonds. Additionally, most RNAs in the cell are relatively short, while DNA can be up to 250 million...
RNA Structure01:19

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
There are three main types of ribonucleic acid (RNA) involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). All three...
RNA Structure01:23

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Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
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Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

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Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
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π-π Interactions in structural stability: role in RNA binding proteins.

V Sivasakthi1, Anand Anbarasu, Sudha Ramaiah

  • 1Bioinformatics Division, School of Biosciences and Technology, VIT University, Vellore, 632014, Tamil Nadu, India.

Cell Biochemistry and Biophysics
|March 26, 2013
PubMed
Summary

Aromatic residues in RNA binding proteins primarily engage in π-π interactions, crucial for protein stability and function. These interactions, particularly side chain-to-side chain, are evolutionarily conserved and vital for global protein structure.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • RNA binding proteins are essential for numerous biological processes.
  • Aromatic amino acid residues, including phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp), play critical roles in protein function.
  • Understanding the interactions involving these residues is key to deciphering protein behavior.

Purpose of the Study:

  • To analyze the role and prevalence of π-π interactions involving aromatic residues in RNA binding proteins.
  • To investigate the types and significance of these interactions for protein structure and stability.

Main Methods:

  • Analysis of residue composition in a dataset of RNA binding proteins.
  • Identification and quantification of aromatic residues (Phe, Tyr, Trp).
  • Mapping and classification of π-π interactions, distinguishing between side chain-side chain and other types.

Main Results:

  • A total of 3,396 aromatic residues were identified, with Phe, Tyr, and Trp comprising 1,547, 1,241, and 608, respectively.
  • A significant majority of these aromatic residues (945 Phe, 634 Tyr, 356 Trp) are involved in π-π interactions.
  • Side chain-to-side chain π-π interactions are the most common type, stabilizing protein cores.
  • π-π interacting residues exhibit evolutionary conservation and possess higher long-range contacts, contributing to global conformational stability.

Conclusions:

  • π-π interactions are a dominant force among aromatic residues in RNA binding proteins.
  • These interactions are critical for maintaining the structural integrity and stability of RNA binding proteins.
  • The evolutionary conservation of these interacting residues underscores their functional importance.