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Gene Families

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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
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Protein and Protein Structure

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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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Protein Families

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Related Experiment Video

Updated: Jul 10, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

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Development of a heme protein structure-electrochemical function database.

Charles J Reedy¹, Margaret M Elvekrog, Brian R Gibney

¹Department of Chemistry, Columbia University, 3000 Broadway, MC 3121, New York, NY 10027, USA.

Nucleic Acids Research

|October 16, 2007

Summary

The Heme Protein Database (HPD) unifies structural data and reduction potentials for heme proteins. This resource reveals how protein fold, heme type, and axial ligands collectively influence heme protein function.

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Measurement of Heme Synthesis Levels in Mammalian Cells

Measurement of Heme Synthesis Levels in Mammalian Cells

Published on: July 9, 2015

Area of Science:

Biochemistry
Structural Biology
Bioinformatics

Background:

Heme proteins are crucial biomolecules with diverse functions.
Existing literature details numerous heme protein structures and functions.
Heme protein reduction potentials (E(m)) vary widely (-550 mV to +450 mV vs. SHE).

Purpose of the Study:

To create a centralized, web-searchable resource for heme protein structure-function relationships.
To integrate structural classifications with reduction potential data.
To facilitate global analysis of heme protein properties.

Main Methods:

Development of the Heme Protein Database (HPD).
Inclusion of structural classifications: protein fold, heme type, and heme axial ligands.
Linking structural data with experimentally determined reduction potential values.

Main Results:

The HPD is the first database to combine these specific heme protein attributes.
Protein fold modulates E(m) over a 300 mV range.
Heme type influences E(m) by up to 600 mV.
Axial ligands contribute to an 800 mV range in E(m).

Conclusions:

The wide 1 V range of heme protein reduction potentials is due to combinations of structural factors.
The HPD provides a valuable tool for understanding heme protein structure-function dynamics.
Subtle interplay between protein fold, heme type, and ligands fine-tunes heme protein redox properties.