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Related Concept Videos

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.
Protein Organization01:13

Protein Organization

Overview
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 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

Protein Folding

Overview

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A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

Protein structure prediction from sequence variation.

Debora S Marks1, Thomas A Hopf, Chris Sander

  • 1Department of Systems Biology, Harvard Medical School, Boston, Massachusetts, USA. ecreview@hms.harvard.edu

Nature Biotechnology
|November 10, 2012
PubMed
Summary
This summary is machine-generated.

Genomic data reveals evolutionary couplings between protein residues, aiding in predicting 3D protein structures. This method also identifies key functional sites and protein dynamics.

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Area of Science:

  • Genomics
  • Computational Biology
  • Structural Biology

Background:

  • Genomic sequences encode evolutionary information crucial for understanding protein function and structure.
  • Predicting three-dimensional (3D) protein structures from amino acid sequences remains a significant challenge in molecular biology.
  • Advances in sequencing technologies and statistical methods have opened new avenues for analyzing evolutionary constraints.

Purpose of the Study:

  • To leverage evolutionary information within genomic sequences for predicting protein 3D structures.
  • To identify evolutionary couplings between amino acid residues in proteins.
  • To explore the utility of covariation analysis in understanding protein function and dynamics.

Main Methods:

  • Mining genomic sequences to detect evolutionary couplings between protein residues.
  • Applying global statistical methods to analyze large datasets of protein sequences.
  • Utilizing computational approaches to infer protein structure and functional sites.

Main Results:

  • Demonstrated the effectiveness of mining genomic sequences for evolutionary information.
  • Successfully identified evolutionary couplings between residues, contributing to 3D structure prediction.
  • Showcased the potential of covariation analysis to identify functionally important residues.

Conclusions:

  • Computational analysis of evolutionary couplings from genomic data significantly advances protein structure prediction.
  • Covariation patterns provide insights into protein functional sites, ligand binding, and complex formation.
  • This approach complements experimental structural biology, offering a comprehensive view of protein structure, function, and evolution.