ISSN:
0006-3592
Keywords:
aggregation
;
folding intermediates
;
inclusion body
;
polymerization
;
protein folding
;
protein-protein interactions
;
self-assembly
;
P22 tailspike protein
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
The misfolding of polypeptide chains and aggregation into the insoluble inclusion body state is a serious problem for biotechnology and biomedical research. Developing a rational strategy to control aggregation requires understanding the mechanism of polymerization. We investigated the in vitro aggregation of P22 tailspike polypeptide chains by classical light scattering, nondenaturing gel electrophoresis, two-dimensional polyacrylamide gel electrophoresis (PAGE), and computer simulations. The aggregation of polypeptide chains during refolding occurred by multimeric polymerization, in which two multimers of any size could associate to form a larger aggregate and did not require a sequential addition of monomeric subunits. The cluster-cluster polymerization mechanism of aggregation is an important determinant in the kinetic competition between productive folding and inclusion body formation. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 54: 333-343, 1997.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
