Editing Protein design (section)

===Design of globular proteins===

[[Globular protein]]s are proteins that contain a hydrophobic core and a hydrophilic surface. Globular proteins often assume a stable structure, unlike [[fibrous protein]]s, which have multiple conformations. The three-dimensional structure of globular proteins is typically easier to determine through [[X-ray crystallography]] and [[nuclear magnetic resonance]] than both fibrous proteins and [[membrane protein]]s, which makes globular proteins more attractive for protein design than the other types of proteins. Most successful protein designs have involved globular proteins. Both [[#Sequence space|RSD-1]], and [[#Target structure|Top7]] were ''de novo'' designs of globular proteins. Five more protein structures were designed, synthesized, and verified in 2012 by the Baker group. These new proteins serve no biotic function, but the structures are intended to act as building-blocks that can be expanded to incorporate functional active sites. The structures were found computationally by using new heuristics based on analyzing the connecting loops between parts of the sequence that specify secondary structures.<ref>{{cite news |title=Proteins made to order |author=Jessica Marshall |url=http://www.nature.com/news/proteins-made-to-order-1.11767 |newspaper=Nature News |date=November 7, 2012 |access-date=November 17, 2012}}</ref>