Do viral proteins possess unique biophysical features?
Natural selection shapes the sequence, structure and biophysical properties of proteins to fit their environment. We hypothesize that highly thermostable proteins and viral proteins represent two opposing adaptation strategies. Thermostable proteins are highly compact and possess well-packed hydrophobic cores and intensely charged surfaces. By contrast, viral proteins, and RNA viral proteins in particular, display a high occurrence of disordered segments and loosely packed cores. These features might endow viral proteins with increased structural flexibility and effective ways to interact with the components of the host. They could also be related to high adaptability levels and mutation rates observed in viruses, thus, representing a unique strategy for buffering the deleterious effects of mutations, such that those that have little (interactions), have little to lose.
Tokuriki
Nobuhiko
N
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
Oldfield
Christopher J
CJ
Uversky
Vladimir N
VN
Berezovsky
Igor N
IN
Tawfik
Dan S
DS
D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D013816:Thermodynamics; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
D014764:Viral Proteins