Number of domains a protein typically folds into as dependent on size

Range 10 to 30 kDa a single domain: Peptides larger than 50 kDa two or more domains domains
Organism Generic
Reference Erickson HP. Size and shape of protein molecules at the nanometer level determined by sedimentation, gel filtration, and electron microscopy. Biol Proced Online. 2009 May 15 11: 32-51. doi: 10.1007/s12575-009-9008-x. p.32 bottom paragraphPubMed ID19495910
Comments "Most proteins fold into globular domains. Protein folding is driven largely by the hydrophobic effect, which seeks to minimize contact of the polypeptide with solvent. Most proteins fold into globular domains, which have a minimal surface area. Peptides from 10 to 30 kDa typically fold into a single domain. Peptides larger than 50 kDa typically form two or more domains that are independently folded."
Entered by Uri M
ID 110566