10 to 30 kDa a single domain: Peptides larger than 50 kDa two or more domains domains
||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
||"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."