[A protein with missing information about its tertiary structure folds into the compact globular structure].
It has been shown by the methods of hydrodynamics (equilibrium ultracentrifugation, velocity sedimentation, intrinsic viscosity) that a fragment of the structural protein Cafl (Cafl 13.149) from the pili-like fibril Yersinia pestis is in the monomeric state and is capable of forming the compact ternary structure spontaneously, without the involvement of chaperone or other subunits. This happens despite the fact that some information about the ternary structure of this protein is provided in fibrils by the "sticky" segment Alal-Thr12 of the neighboring subunit. As previously shown, it is this segment of another molecule in the norm that is an important element of the ternary structure of the subunit itself since it interacts with the acceptor cleft and participates in the formation of the hydrophobic core.
V M
VM
Tishchenko
D001426:Bacterial Proteins / Q000737:chemistry*; D008970:Molecular Weight; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D012997:Solvents; D014783:Viscosity; D015010:Yersinia pestis / Q000737:chemistry*
D001426:Bacterial Proteins; D021122:Protein Subunits; D012997:Solvents; C086725:caf1 protein, Yersinia pestis