Computer Science
Scientific paper
Jul 1993
adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1993adspr..13..251c&link_type=abstract
Advances in Space Research, Volume 13, Issue 7, p. 251-257.
Computer Science
6
Scientific paper
The coat of polyomavirus is composed of three proteins that can self-assemble to form an icosahedral capsid. VP1 represents 75% of the virus capsid protein and the VP1 capsomere subunits are capable of self assembly to form a capsid-like structure. Ground-based and orbiter studies were conducted with VP1 protein cloned in an expression vector and purified to provide ample quantities for capsomere-capsid assembly. Flight studies were conducted on STS-37 on April 5-9, 1991. Assembly initiated when a VP1 protein solution was interfaced with a Ca+2 buffer solution (pH 5.0). After four days a second alignment terminated the assembly process and allowed for glutaraldehyde fixation. Flight and ground-based samples were analyzed by electron microscopy. Ground-based experiments revealed the assembly of VP1 into capsid-like structures and a heterogenous size array of capsomere subunits. Samples reacted in microgravity, however, showed capsomeres of a homogenous size, but lack of capsid-like assembly.
Chang Darwin
Consigli Richard A.
Johnson Timothy C.
Paulsen Avelina
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