title: Globularity and protein function.
abstract: Abstract   The forces that direct protein folding lead naturally to native proteins and protein domains that are typically, to a first approximation, globular-spherical and compact, with a relatively clear distinction between the hydrophobic inside and polar outside. The near-universality of these features of protein structures sharpens our focus on some apparent exceptions. Consideration of the structure/function link in some of the exceptional cases provides some insights into our views of protein function.
authors.affiliation: a      Chemistry Department   ,  Princeton University   ,    Princeton   ,    NJ   ,    08544-1009.
authors.forename: J
authors.initials: J
authors.lastname: Carey
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry
chemical_list: D011506:Proteins