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Related Concept Videos

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 Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
Protein Families02:47

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key locations, protein...
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

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Updated: Jun 12, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Heme proteins--diversity in structural characteristics, function, and folding.

Lorna J Smith1, Abdullah Kahraman, Janet M Thornton

  • 1Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, Oxford OX1 3QR, United Kingdom. lorna.smith@chem.ox.ac.uk

Proteins
|June 15, 2010
PubMed
Summary
This summary is machine-generated.

Heme protein structure dictates function. Proteins with permanent heme binding show unfolded apo states, while transient binders remain folded, impacting biological activity and stability.

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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Published on: September 2, 2019

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Last Updated: Jun 12, 2026

Measurement of Heme Synthesis Levels in Mammalian Cells
09:43

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
08:58

In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Heme proteins are crucial for diverse biological functions.
  • The heme prosthetic group and its binding site are key determinants of protein activity.
  • Understanding heme-protein interactions is vital for protein design and function prediction.

Purpose of the Study:

  • To analyze the relationship between heme binding site characteristics and protein function.
  • To investigate the structural properties of apo states in relation to heme binding modes.
  • To establish principles for designing novel heme-binding proteins and identifying functions of unknown heme proteins.

Main Methods:

  • Analysis of a diverse dataset of nonhomologous heme proteins.
  • Characterization of heme binding site variations (shape, volume, composition).
  • Assessment of heme-protein interactions and apo state structures.

Main Results:

  • Significant variations in heme environments correlate with distinct protein functions.
  • Proteins with permanent heme binding exhibit disordered apo states (local to complete unfolding).
  • Proteins with transient heme binding maintain folded structures in both apo and holo states, enhancing stability and activity.

Conclusions:

  • Heme binding site characteristics significantly influence protein function and apo state stability.
  • The observed principles provide a foundation for rational de novo protein design for specific heme-binding properties.
  • This framework aids in elucidating the roles of uncharacterized proteins containing heme ligands.