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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
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...
Protein Folding01:22

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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.
A protein's shape is critical to its function. For example, an enzyme can...
Protein Organization01:13

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Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Related Experiment Video

Updated: May 7, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Exploiting tertiary structure through local folds for crystallographic phasing.

Massimo Sammito1, Claudia Millán, Dayté D Rodríguez

  • 1Instituto de Biología Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Barcelona, Spain.

Nature Methods
|September 17, 2013
PubMed
Summary
This summary is machine-generated.

A new algorithm uses Protein Data Bank fragments to solve protein crystal X-ray diffraction data. This method successfully phases diverse protein structures, offering a valuable tool for structural biology research.

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Last Updated: May 7, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

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Published on: May 13, 2020

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Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Protein structure determination is crucial for understanding biological function.
  • X-ray crystallography is a primary method for determining protein structures.
  • Phasing X-ray diffraction data remains a bottleneck in the crystallographic process.

Purpose of the Study:

  • To develop and present a novel algorithm for phasing protein crystal X-ray diffraction data.
  • To leverage existing structural information from the Protein Data Bank (PDB).
  • To provide a robust computational tool for solving challenging protein structures.

Main Methods:

  • An algorithm was developed to identify, retrieve, refine, and utilize tertiary structural information from small protein fragments.
  • Unspecific molecular replacement was combined with density modification techniques.
  • The method was tested on various protein structural classes, including all-helical, mixed alpha-beta, and all-beta proteins.

Main Results:

  • The algorithm successfully phased diverse protein crystal X-ray diffraction datasets.
  • The method demonstrated effectiveness across different protein structural architectures.
  • The developed algorithm, named Borges, proved capable of handling complex phasing challenges.

Conclusions:

  • The described algorithm provides an effective solution for phasing protein crystal X-ray diffraction data.
  • Exploiting general tertiary structural information from PDB fragments is a viable strategy for phasing.
  • The Borges software implementation offers a practical tool for the structural biology community.