Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs.
Helical integral membrane proteins share several structural determinants that are widely conserved across their universe. The discovery of common motifs has furthered our understanding of the features that are important to stability in the membrane environment, while simultaneously providing clues about proteins that lack high-resolution structures. Motif analysis also helps to target mutagenesis studies, and other experimental and computational work. Three types of transmembrane motifs have recently seen interesting developments: the GxxxG motif and its like; polar and hydrogen bonding motifs; and proline motifs.
Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6059, USA.
Alessandro
A
Senes
Donald E
DE
Engel
William F
WF
DeGrado
D020816:Amino Acid Motifs; D005998:Glycine / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011392:Proline / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D008565:Membrane Proteins; D011392:Proline; D005998:Glycine