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Defining the Stability of Multimeric Proteins
2008The practical application of scanning calorimetry and spectroscopic methods to measure the stability of multimeric proteins is described. Oligomeric proteins are stabilized by both the intrinsic folding energy of the subunits as well as interactions between the subunits.
John W, Shriver, Stephen P, Edmondson
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A Rainbow Trout Lectin with Multimeric Structure
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1997A novel lectin has been identified in rainbow trout serum and plasma. The lectin binds to Sepharose (an agarose polymer) in a calcium-dependent manner. Glucose, N-acetyl-glucosamine, mannose, N-acetyl-mannosamine, L-fucose, maltose and alpha-methyl-mannoside are good inhibitors of this binding, whereas glucosamine and D-fucose inhibits to a lesser ...
Jensen, L E +3 more
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Colicin A multimerizes when unfolded
Biochimie, 2002A purified preparation of colicin A produced by Escherichia coli cells contained various forms of colicin A. Unfolding of the purified colicin A with urea provoked multimerization. Dimers, tetramers and hexamers of colicin A were identified.
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The functional significance of multimerization in ion channels
Current Opinion in Structural Biology, 1998Recently, the allosteric behavior of ion channels has been investigated by recording the individual steps leading to the complete activation of a cyclic nucleotide-gated ion channel. This information, in combination with recent studies on nicotinic acetylcholine receptor mutants, necessitates a modification of our current theories of the allosteric ...
M L, Tierney, M H, Stowell
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Abstract Rather than operating as monomers, proteins often assemble into multimeric structures. Homomers, constructed from proteins encoded by the same gene, are about twice as frequent as heteromers, with the frequencies of types declining with increasing numbers of subunits per multimer.
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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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Hitting multiple targets with multimeric ligands
Expert Opinion on Therapeutic Targets, 2004Multimeric ligands consist of multiple monomeric ligands attached to a single backbone molecule, creating a multimer that can bind to multiple receptors or targets simultaneously. Numerous examples of multimeric binding exist within nature. Due to the multiple and simultaneous binding events, multimeric ligands bind with an increased affinity compared ...
Heather L, Handl +5 more
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Multimeric Analysis of von Willebrand Factor
2003Von Willebrand Factor (vWF) in normal plasma is composed of a series of high molecular multimers, ranging in size from 8×10(5) to over 15×10(6) Daltons (1). The multimeric structure of vWF was first investigated by two-dimensional crossed immunoelectrophoresis (2D-IEP). In 1974, Kernoff et al. (2) used this method, and since then multimer sizing of von
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