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In structural biology, a protomer is the structural unit of an oligomeric protein. It is the smallest unit composed of at least two different protein chains that form a larger heterooligomer by association of two or more copies of this unit.

The term was introduced by Chetverin [1] to make nomenclature in Na/K-ATPase unambiguous. Na/K-consists of an α- and a β-subunit (plus a proteolipid, called γ-subunit). At the time it was unclear how many of each work together. In addition, when people spoke of a dimer, did they refer to αβ or to (αβ)2? Chetverin suggested to call αβ a protomer and (αβ)2 a diprotomer.

Protomers usually arrange in cyclic symmetry to form closed point group symmetries.


Hemoglobin is a heterotetramer consisting of four subunits (two α and two β). However, structurally and functionally hemoglobin is described better as (αβ)2, we say it is a dimer of two αβ-protomers, that is, a diprotomer.[2]

Aspartate carbamoyltransferase has a α6β6 subunit composition. The six αβ-protomers are arranged in D3 symmetry.

Viral capsid often are made from protomers.


  1. ^ Chetverin, A.B. (1986). "Evidence for a diprotomeric structure of Na, K-ATPase: Accurate determination of protein concentration and quantitative end-group analysis". FEBS Lett. 196: 121–125. doi:10.1016/0014-5793(86)80225-3. PMID 3002859. 
  2. ^ Buxbaum, E. (2007). Fundamentals of protein structure and function. New York: Springer. pp. 105–120. ISBN 978-0-387-26352-6. 

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