TY - JOUR
T1 - Hydrophobic patches on the surfaces of protein structures
AU - Lijnzaad, Philip
AU - Berendsen, Herman J.C.
AU - Argos, Patrick
PY - 1996
Y1 - 1996
N2 - A survey of hydrophobic patches on the surface of 112 soluble, monomeric proteins is presented. The largest patch on each individual protein averages around 400 Å2 but can range from 200 to 1,200 Å2. These areas are not correlated to the sizes of the proteins and only weakly to their apolar surface fraction. Ala, Lys, and Pro have dominating contributions to the apolar surface for smaller patches, while those of the hydrophobic amino acids become more important as the patch size increases. The hydrophilic amino acids expose an approximately constant fraction of their apolar area independent of patch size; the hydrophobic residue types reach similar exposure only in the larger patches. Though the mobility of residues on the surface is generally higher, it decreases for hydrophilic residues with increasing patch size. Several characteristics of hydrophobic patches catalogued here should prove useful in the design and engineering of proteins.
AB - A survey of hydrophobic patches on the surface of 112 soluble, monomeric proteins is presented. The largest patch on each individual protein averages around 400 Å2 but can range from 200 to 1,200 Å2. These areas are not correlated to the sizes of the proteins and only weakly to their apolar surface fraction. Ala, Lys, and Pro have dominating contributions to the apolar surface for smaller patches, while those of the hydrophobic amino acids become more important as the patch size increases. The hydrophilic amino acids expose an approximately constant fraction of their apolar area independent of patch size; the hydrophobic residue types reach similar exposure only in the larger patches. Though the mobility of residues on the surface is generally higher, it decreases for hydrophilic residues with increasing patch size. Several characteristics of hydrophobic patches catalogued here should prove useful in the design and engineering of proteins.
KW - lipophilicity
KW - molecular recognition
KW - molecular surface
UR - http://www.scopus.com/inward/record.url?scp=0030055023&partnerID=8YFLogxK
U2 - 10.1002/(SICI)1097-0134(199607)25:3<389::AID-PROT10>3.3.CO;2-S
DO - 10.1002/(SICI)1097-0134(199607)25:3<389::AID-PROT10>3.3.CO;2-S
M3 - Article
C2 - 8844873
AN - SCOPUS:0030055023
SN - 0887-3585
VL - 25
SP - 389
EP - 397
JO - Proteins: Structure, Function and Genetics
JF - Proteins: Structure, Function and Genetics
IS - 3
ER -