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2/1/09 9:42 PMQuaternary structure - Wikipedia, the free encyclopediaPage 1 of 4http://en.wikipedia.org/wiki/Quaternary_structure
Quaternary structure
From Wikipedia, the free encyclopedia
In biochemistry,
quaternary structure
is the arrangement of multiple folded protein molecules in a multi-subunit complex.
Contents
1 Description and examples2Nomenclature of quaternary structures3 Determination of quaternary structure3.1 Methods that measure mass of intact complex directly 3.2 Methods that measure the size of the intact complex directly3.3 Methods that measure the size of the intact complex indirectly4 Protein-protein interactions5 Quaternary or Quartary?6See also7References8External links
Description and examples
Many proteins are actually assemblies of more than one polypeptide chain, which in the context of the largerassemblage are known as protein subunits. In addition to the tertiary structure of the subunits, multiple-subunitproteins possess a
quaternary structure
, which is the arrangement into which the subunits assemble.Enzymes composed of subunits with diverse functions are sometimes called holoenzymes, in which some partsmay be known as regulatory subunits and the functional core is known as the catalytic subunit. Examples of proteins with quaternary structure include hemoglobin, DNA polymerase, and ion channels. Other assembliesreferred to instead as
multiprotein complexes
also possess quaternary structure. Examples include nucleosomes and microtubules. Changes in quaternary structure can occur through conformational changes within individualsubunits or through reorientation of the subunits relative to each other. It is through such changes, whichunderlie cooperativity and allostery in "multimeric" enzymes, that many proteins undergo regulation andperform their physiological function.The above definition follows a classical approach to biochemistry, established at times when the distinctionbetween a protein and a functional, proteinaceous unit was difficult to elucidate. More recently, people refer toprotein-protein interaction when discussing quaternary structure of proteins and consider all assemblies of proteins as protein complexes.
 
2/1/09 9:42 PMQuaternary structure - Wikipedia, the free encyclopediaPage 2 of 4http://en.wikipedia.org/wiki/Quaternary_structure
Nomenclature of quaternary structures
The number of subunits in an oligomeric complex are described using names that end in -mer (Greek for "part,subunit"). Formal Greco-Latinate names are generally used for the first ten types and can be used for up totwenty subunits, whereas higher order complexes are usually described by the number of subunits, followed by-meric.1 = monomer2 = dimer3 = trimer4 = tetramer5 = pentamer6 = hexamer7 = heptamer8 = octamer9 = nonamer10 = decamer11 = undecamer12 = dodecamer13 = tridecamer14 = tetradecamer15 = pentadecamer*16 = hexadecamer17 = heptadecamer*18 = octadecamer19 = nonadecamer20 = eicosamer21-mer22-mer23-mer*etc.*
 No known examples
Although complexes higher than octamers are rarely observed for most proteins, there are some importantexceptions. Viral capsids are often composed of multiples of 60 proteins. Several molecular machines are alsofound in the cell, such as the proteasome (four heptameric rings = 28 subunits), the transcription complex andthe spliceosome. The ribosome is probably the largest molecular machine, and is composed of many RNA andprotein molecules.In some cases, proteins form complexes that then assemble into even larger complexes. In such cases, one usesthe nomenclature, e.g., "dimer of dimers" or "trimer of dimers", to suggest that the complex might dissociateinto smaller sub-complexes before dissociating into monomers.
Determination of quaternary structure
Protein quaternary structure can be determined using a variety of experimental techniques that require asample of protein in a variety of experimental conditions. The experiments often provide an estimate of themass of the native protein and, together with knowledge of the masses and/or stoichiometry of the subunits,allow the quaternary structure to be predicted with a given accuracy. It is not always possible to obtain aprecise determination of the subunit composition for a variety of reasons.The number of subunits in a protein complex can often be determined by measuring the hydrodynamicmolecular volume or mass of the intact complex, which requires native solution conditions. For
 folded 
proteins, the mass can be inferred from its volume using the partial specific volume of 0.73 ml/g. However,olume measurements are less certain than mass measurements, since
unfolded 
proteins appear to have a muchlarger volume than folded proteins; additional experiments are required to determined whether a protein isunfolded or has formed an oligomer.
Methods that measure mass of intact complex directly
 
2/1/09 9:42 PMQuaternary structure - Wikipedia, the free encyclopediaPage 3 of 4http://en.wikipedia.org/wiki/Quaternary_structure
sedimentation-equilibrium analytical ultracentrifugationelectrospray mass spectrometry
Methods that measure the size of the intact complex directly
static light scatteringsize exclusion chromatography (requires calibration)
Methods that measure the size of the intact complex indirectly
sedimentation-velocity analytical ultracentrifugation (measures the translational diffusion constant)dynamic light scattering (measures the translational diffusion constant)pulsed-gradient protein nuclear magnetic resonance (measures the translational diffusion constant)fluorescence polarization (measures the rotational diffusion constant)dielectric relaxation (measures the rotational diffusion constant)Methods that measure the mass or volume under unfolding conditions (such as MALDI-TOF massspectrometry and SDS-PAGE) are generally not useful, since non-native conditions usually cause the complexto dissociate into monomers. However, these may sometimes be applicable; for example, the experimentermay apply SDS-PAGE after first treating the intact complex with chemical cross-linking reagents.
Protein-protein interactions
Proteins are capable of forming very tight complexes. For example, ribonuclease inhibitor binds toribonuclease A with a roughly 20 fM dissociation constant. Other proteins have evolved to bind specifically tounusual moieties on another protein, e.g., biotin groups (avidin), phosphorylated tyrosines (SH2 domains) orproline-rich segments (SH3 domains).
Quaternary or Quartary?
In biology, the non-standard usage "Quaternary structure" is so firmly entrenched that to refer to "Quartarystructure" would be incorrect. The correct term should really be "Quartary":
Quartary
(from Latin:
quartarius
) is the fourth member of an ordinal number word series beginningwith (primary, secondary, tertiary) and continuing with (quintary, sextary, ...).
[1]
Quaternary
(from Latin:
quaternarius
) is the fourth member of a distributive number word seriesbeginning with (singular, binary, ternary) and continuing with (quinary, senary, septenary, octonary ...centenary).
[2][3]
See also
primary structuresecondary structuretertiary structure
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