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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
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Protein Folding

Overview
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Viral Structure00:56

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Related Experiment Video

Updated: May 20, 2026

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit
22:10

Multi-target Parallel Processing Approach for Gene-to-structure Determination of the Influenza Polymerase PB2 Subunit

Published on: June 28, 2013

Dengue virus nonstructural protein 5 adopts multiple conformations in solution.

Cécile Bussetta1, Kyung H Choi

  • 1Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555-0647, USA.

Biochemistry
|July 5, 2012
PubMed
Summary

Full-length Dengue virus nonstructural protein 5 (NS5) exists as multiple conformations in solution. These findings suggest flexible interactions between its two domains, crucial for viral RNA synthesis.

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Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Dengue virus nonstructural protein 5 (NS5) is essential for viral RNA replication.
  • NS5 comprises an N-terminal methyltransferase domain and a C-terminal RNA-dependent RNA polymerase domain.
  • Previous structural studies focused on isolated NS5 domains, leaving the full-length protein's structure and domain interactions uncharacterized.

Purpose of the Study:

  • To investigate the solution structure and dynamics of full-length Dengue virus type 3 NS5.
  • To determine if the two NS5 domains interact and adopt a fixed relative orientation.

Main Methods:

  • Small-angle X-ray scattering (SAXS) experiments were performed on full-length DENV-3 NS5.
  • Analysis of SAXS data to infer the protein's conformation and quaternary structure in solution.

Main Results:

  • Full-length DENV-3 NS5 was found to be monomeric and well-folded in solution.
  • SAXS data indicated that NS5 adopts multiple conformations, varying from compact to extended forms.
  • The two domains of NS5 do not appear to interact strongly, suggesting flexibility.

Conclusions:

  • DENV NS5 exhibits conformational flexibility in solution, likely due to weak inter-domain interactions and linker flexibility.
  • This conformational plasticity may be important for its function in the viral replication complex.