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Hemoglobin

Hemoglobin

Hemoglobin is a globular protein made up of four subunits. Two of these subunits are alpha chains, and the other two are beta chains. Each subunit contains a molecule of heme, which has an iron atom and can bind to oxygen. When an oxygen molecule binds to one heme group, it changes the shape of hemoglobin, making it easier for the other heme groups to bind oxygen as well.
When all four heme groups are bound to oxygen, the resulting molecule is called oxyhemoglobin. As a result, arterial blood...

Oxygen Transport in the Blood

Oxygen Transport in the Blood

Hemoglobin (Hb) is a crucial molecule in the human body, consisting of four polypeptide chains, each bound to an iron-containing heme group. This unique structure enables hemoglobin to bind to oxygen, with each molecule capable of combining with four molecules of oxygen, leading to rapid and reversible oxygen loading. When fully loaded with oxygen, it is called oxyhemoglobin, while hemoglobin that has released oxygen is called reduced hemoglobin or deoxyhemoglobin. As hemoglobin binds oxygen,...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Gene Families

Gene Families

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.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

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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...

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Related Experiment Video

Updated: Mar 12, 2026

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

A Precision Medicine Tool for Measurement and Monitoring of Hemoglobin S in Sickle Cell Disease Patients Receiving Transfusion Therapy

Predictable convergence in hemoglobin function has unpredictable molecular underpinnings.

Chandrasekhar Natarajan¹, Federico G Hoffmann², Roy E Weber³

¹School of Biological Sciences, University of Nebraska, Lincoln, NE 68588, USA.

Science (New York, N.Y.)

|November 16, 2016

Summary

This summary is machine-generated.

Genetic adaptation shows predictable functional changes but unpredictable molecular roots. Historical mutations and genetic backgrounds limit evolutionary pathways, meaning adaptive solutions are not universal across species.

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Last Updated: Mar 12, 2026

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Area of Science:

Evolutionary biology
Molecular evolution
Biochemistry

Background:

Genetic adaptation drives evolutionary change.
Hemoglobin-oxygen affinity is crucial for high-altitude survival.
Understanding convergence reveals evolutionary predictability.

Purpose of the Study:

Investigate the predictability of genetic adaptation.
Examine the molecular basis of convergent hemoglobin function evolution.
Assess the role of historical contingency in adaptation.

Main Methods:

Comparative analysis of 56 avian taxa with differing altitudinal ranges.
Amino acid substitution analysis in hemoglobin.
Experiments with resurrected ancestral proteins.

Main Results:

Convergent increases in hemoglobin-oxygen affinity were common in high-altitude birds.
Few convergent functional changes resulted from parallel amino acid substitutions.
Historical substitutions had context-dependent effects on protein function.
Genetic background influenced the adaptive potential of mutations.

Conclusions:

Biochemical phenotypes can show predictable adaptation.
The molecular basis for adaptation is not always predictable.
Evolutionary adaptation is constrained by historical contingency and genetic background.