Study of a Circular RFQ Storage and Accelerator Ring - Digital Library
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Ruggiero, A. G.
Study of a Circular RFQ Storage and Accelerator Ring,
October 1, 2001;
United States.
accessed February 11, 2018),
University of North Texas Libraries, Digital Library, ;
crediting UNT Libraries Government Documents Department.Phage display of intact domains at high copy number: A system based on SOC, the small outer capsid protein of bacteriophage T4 - Ren - 1996 - Protein Science - Wiley Online Library
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Peptides fused to the coat proteins of filamentous phages have found widespread applications in antigen display, the construction of antibody libraries, and biopanning. However, such systems are limited in terms of the size and number of the peptides that may be incorporated without compromising the fusion proteins' capacity to self-assemble. We describe here a system in which the molecules to be displayed are bound to pre-assembled polymers. The polymers are T4 capsids and polyheads (tubular capsid variants) and the display molecules are derivatives of the dispensable capsid protein SOC. In one implementation, SOC and its fusion derivatives are expressed at high levels in Escherichia coli, purified in high yield, and then bound in vitro to separately isolated polyheads. In the other, a positive selection vector forces integration of the modified soc gene into a soc-deleted T4 genome, leading to in vivo binding of the display protein to progeny virions. The system is demonstrated as applied to C-terminal fusions to SOC of (1) (2) the 43-residue V3 loop domain of gpl20, the human immunodeficiency virus type-1 (HIV-1) e and (3) poliovirus VP1 capsid protein (312 residues). SOC-V3 displaying phage were highly antigenic in mice and produced antibodies reactive with native gp120. That the fusion protein binds correctly to the surface lattice was attested in averaged electron micrographs of polyheads. The SOC display system is capable of presenting up to & 103 copies per capsid and &104 copies per polyhead of V3-sized domains. Phage displaying SOC-VP1 were isolated from a 1:106 mixture by two cycles of a simple biopanning procedure, indicating that proteins of at least 35 kDa may be accommodated.
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Export JavaScript is disabled on your browser. Please enable JavaScript to use all the features on this page., November 1998, Pages 129-153Author links open overlay panelShow moreopen archiveAbstractThe paper presents a permutation procedure for testing reflected (or diagonal) symmetry of the distribution of a multivariate variable. The test statistics are based in empirical characteristic functions. The resulting permutation tests are strictly distribution free under the null hypothesis that the underlying variables are symmetrically distributed about a center. Furthermore, the permutation tests are strictly valid if the symmetric center is known and are asymptotic valid if the center is an unknown point. The equivalence, in the large sample sense, between the tests and their permutation counterparts are established. The power behavior of the tests and their permutation counterparts under local alternative are investigated. Some simulations with small sample sizes (?20) are conducted to demonstrate how the permutation tests works.Keywordsempirical characteristic function, empirical process, permutation tests, reflected symmetry, validity of testRecommended articlesCiting articles (0)