NATIVE GLOBULAR AND NATIVE PARTIALLY OR COMPLETELY DISORDERED PROTEINS. FOLDING, SUPRAMOLECULAR COMPLEX FORMATION
AND AGGREGATION
K. K. Turoverov,1 V. N. Uverslcy,2 I. M. Kuznetsova 1
1 Laboratory of structural dynamics, stability and folding of proteins, Institute of Cytology RAS,
St. Petersburg, Russia, and 2 Institute for Intrinsically Disordered Protein Research, Center for Computational Biology
and Bioinformatics, Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, USA;
e-mail: 1 kkt@mail.cytspb.rssi.ru
2 vuversky@iupui.edu
Recently it became evident that proteins can perform their function not only in globular state but also in partially or completely disordered state. The majority of
globular proteins are enzymes which function is strictly determined. Regulation and signaling proteins participating in interconnection with variety of partners must
have much more lability, and macromolecules of such proteins are mainly in partially or completely disordered state. The aim of this work was to describe from the
unified viewpoint in the frame of energy landscape model the existence of native globular, native partially or completely disordered proteins, formation of intermolecular
complexes with various partners, formation of amorphous aggregates and amyloid fibrils. Compact globular proteins are formed if polypeptide chain provides strong
intramolecular interconnections. The ability of polypeptide chain to fold in a compact globule depends on the relation of hydrophobic and charged aminoacids in its
composition. Many partially or completely disordered proteins can form compact structure in complexes with their partners, which are composed by mtermolecular
interactions of polypeptide chains of protein and its partner. Intermolecular interaction of proteins can lead to formation associates, amorphous aggregates, amyloid
and amyloid-like fibrils. The requisite condition of such contact formation is the availability of hydrophobic clusters of polypeptide chain exposed to the solution.
That is why aggregation of partially or completely disordered proteins is more favorable in comparison with globular proteins.
Key words: protein folding, globular proteins, natively disordered proteins, protein-protein and DNA-protein complexes, amorphous aggregates,
amyloid fibrils, inter- and intramolecular contacts
Back
Contents
Main
|
