Unfolding domains of recombinant fusion αα-tropomyosin
نویسندگان
چکیده
منابع مشابه
The Periodic Unfolding Method in Perforated Domains
The periodic unfolding method was introduced in [4] by D. Cioranescu, A. Damlamian and G. Griso for the study of classical periodic homogenization. The main tools are the unfolding operator and a macro-micro decomposition of functions which allows to separate the macroscopic and microscopic scales. In this paper, we extend this method to the homogenization in domains with holes, introducing the...
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Human serum albumin (HSA) contains three alpha-helical domains (I-III). The unfolding process of these domains was monitored using covalently bound fluorescence probes; domain I was monitored by N-(1-pyrene)maleimide (PM) conjugated with cys-34, domain II was monitored by the lone tryptophan residue and domain III was followed by p-nitrophenyl anthranilate (NPA) conjugated with Tyrosine-411 (Ty...
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Fibroblast caldesmon is a protein postulated to participate in the modulation of the actin cytoskeleton and the regulation of actin-based motility. The cDNAs encoding the NH2-terminal (aa.1-243, CaD40) and COOH-terminal (aa.244-538, CaD39) fragments of human caldesmon were subcloned into expression vectors and we previously reported that bacterially produced CaD39 protein retains its actin-bind...
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Titin, a 1-microm-long protein found in striated muscle myofibrils, possesses unique elastic and extensibility properties in its I-band region, which is largely composed of a PEVK region (70% proline, glutamic acid, valine, and lysine residue) and seven-strand beta-sandwich immunoglobulin-like (Ig) domains. The behavior of titin as a multistage entropic spring has been shown in atomic force mic...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1992
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560011011