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Proc. Natl. Acad. Sci. USA Vol. 96, pp. 94659468, August 1999
 

Summary: Proc. Natl. Acad. Sci. USA
Vol. 96, pp. 9465­9468, August 1999
Physics
Aeolotopic interactions of globular proteins
ALEKSEY LOMAKIN, NEER ASHERIE, AND GEORGE B. BENEDEK*
Department of Physics, Center for Materials Science and Engineering, and Materials Processing Center, Massachusetts Institute of Technology, Cambridge, MA
02139-4307
Contributed by George B. Benedek, June 18, 1999
ABSTRACT Protein crystallization, aggregation, liquid­
liquid phase separation, and self-assembly are important in
protein structure determination in the industrial processing
of proteins and in the inhibition of protein condensation
diseases. To fully describe such phase transformations in
globular protein solutions, it is necessary to account for the
strong spatial variation of the interactions on the protein
surface. One difficulty is that each globular protein has its
own unique surface, which is crucial for its biological function.
However, the similarities amongst the macroscopic properties
of different protein solutions suggest that there may exist a
generic model that is capable of describing the nonuniform

  

Source: Asherie, Neer - Departments of Physics & Biology, Yeshiva University
Benedek, George B. - Department of Physics, Massachusetts Institute of Technology (MIT)

 

Collections: Biology and Medicine; Physics