Results 151 to 160 of about 30,399 (190)
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Folding and association of oligomeric and multimeric proteins
2000Publisher Summary This chapter deals with the formation of the native tertiary and quaternary structure of proteins— that is, with the sequentially ordered folding/ association reaction. In discussing the mechanisms involved in both processes, available information originates exclusively from in vitro denaturation/ renaturation studies, suggesting ...
R, Jaenicke, H, Lilie
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Structures of Multimeric Proteins by NMR
1996Recent advances in NMR methodology, in particular the increase in resolution afforded by the advent of three- and four-dimensional NMR (see Clore & Gronenborn, 1991 for a review) have permitted the structures of proteins in the 15-25 kDa range to be solved in solution.
G. Marius Clore, Angela M. Gronenborn
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Proteins: Structure, Function, and Bioinformatics, 2002
Abstract In this postgenomic era, the ability to identify protein–protein interactions on a genomic scale is very important to assist in the assignment of physiological function. Because of the increasing number of solved structures involving protein complexes, the time is ripe to extend threading to the prediction of quaternary ...
Long, Lu, Hui, Lu, Jeffrey, Skolnick
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Abstract In this postgenomic era, the ability to identify protein–protein interactions on a genomic scale is very important to assist in the assignment of physiological function. Because of the increasing number of solved structures involving protein complexes, the time is ripe to extend threading to the prediction of quaternary ...
Long, Lu, Hui, Lu, Jeffrey, Skolnick
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Spectroscopic studies of the unfolding of a multimeric protein α‐crystallin
Biopolymers, 2014ABSTRACTα‐Crystallin is a multimeric eye lens protein having molecular chaperone‐like function which is crucial for lens transparency. The stability and unfolding‐refolding properties of α‐crystallin plays important roles for its function. We undertook a multi probe based fluorescence spectroscopic approach to explore the changes in the various levels ...
Aritra, Chowdhury +4 more
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Enhancing immunoassay detection of antigens with multimeric protein Gs
Biosensors and Bioelectronics, 2011This paper describes a method for the effective and self-oriented immobilization of antibodies on magnetic silica-nanoparticles using a multimeric protein G. Cysteine-tagged recombinant dimers and trimers of protein G were produced in Escherichia coli BL21 by repeated linking of protein G monomers with a flexible (GGGGS)(3) linker. Amino-functionalized
Jin Hyung, Lee +4 more
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A system for stable indirect immobilization of multimeric recombinant proteins
Immunotechnology, 1998To perform an ELISA or for panning phage particles which display recombinant proteins, one of the reactants is immobilized on solid phase. Immobilization in ELISA is generally performed by passive adsorption of ligands to plastic. However, protein is denatured during the adsorption process.
Grob P, Baumann S, Ackermann M, Suter M
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Functional genomic dissection of multimeric protein families in zebrafish
Developmental Dynamics, 2003AbstractThe study of multimeric protein function in the postgenomicera has become complicated by the discovery of multiple isoforms for each subunit of those proteins. A correspondingly large number of potential isoform combinations offer the multicellular organism a constellation of protein assemblies from which to generate a variety of functions ...
Keith C, Cheng +2 more
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The purified colicin S8 is a multimeric protein.
International microbiology : the official journal of the Spanish Society for Microbiology, 2001Bacteriocins have been isolated both as simple proteins and as proteins in association with carbohydrates, lipids, etc. Colicins are commonly inducible and extracellular. Their molecular masses range from 30 to 90 kDa. Pure colicin S8 was obtained in three steps from supernatant of induced cells: (i) Ammonium sulfate precipitation; (ii) anion exchange ...
J L, Concepción Curbelo +1 more
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Multimerization of the transient receptor proteins TRPV6 and TRPC1
Qatar Foundation Annual Research Forum Proceedings, 2010AbstractTransient Receptor Potential (TRP) ion channels are formed by the juxtaposition of either homomeric or heteromeric assembly of four TRP subunits. TRP proteins have six transmembrane domains (TM) and a P-loop located between TM5 and TM6 that defines the channel pore.
Raphael Jean Courjaret, +2 more
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Assembly of Multimeric Proteins
Journal of Molecular Biology, 1993Suhail Ahmad +2 more
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