A protein lacking an essential input to its tertiary structure does fold into a compact globule |
| |
Authors: | V M Tischenko |
| |
Institution: | 1.Institute of Biological Instrumentation,Russian Academy of Sciences,Pushchino, Moscow Region,Russia |
| |
Abstract: | It is shown by equilibrium ultracentrifugation, velocity sedimentation, and viscometry that an N-truncated structural protein
Caf1 (Cafl13–149) of the Yersinia pestis capsular antigen fiber exists as a monomer in solution and is capable of folding from denatured state into a compact globular
state by itself, without involvement of a chaperone or other subunits. This happens despite the fact that in the norm, important
information on the tertiary structure of each Caf1 subunit (specifically, completion of its hydrophobic core) is provided
by the “donor” segment Ala1-Thr12 of the neighboring fiber subunit. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|