Magnitude and spatial orientation of the hydrophobic moments of multi-domain proteins.
The distributions of residue hydrophobicity for individual domains as well as for the aggregates of domains on a single chain have been found to exhibit well-defined second-order hydrophobic moment profiles. This indicates that most of the domains do fold into a stable entity with a core composed predominantly of hydrophobic residues as well as a prevalence of hydrophobic residues at the interface between domains. A simple scoring function based upon the relative hydrophobic moment dipole orientations shows that 80% of the dipoles of adjacent domains point to each other, highlighting hydrophobic residue prevalence at the domain interfaces.
IBM Thomas J. Watson Research Center, Yorktown Heights, NY 10598, USA. ruhongz@us.ibm.com
Ruhong
R
Zhou
Ajay
A
Royyuru
Prasanna
P
Athma
Frank
F
Suits
D020816:Amino Acid Motifs; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D057927:Hydrophobic and Hydrophilic Interactions; D015233:Models, Statistical; D008968:Molecular Conformation; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D040901:Proteomics / Q000379:methods; D012997:Solvents / Q000737:chemistry
D011506:Proteins; D012997:Solvents