All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins
نویسندگان
چکیده
منابع مشابه
Sugar-induced molten-globule model.
Proteins denature at low pH because of intramolecular electrostatic repulsions. The addition of salt partially overcomes this repulsion for some proteins, yielding a collapsed conformation called the A-state. A-states have characteristics expected for the molten globule, a notional kinetic protein folding intermediate. Here we show that the addition of neutral sugars to solutions of acid-denatu...
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The reversible heat- and GuHCl-induced unfolding of bovine serum fetuin (BSF) has been studied by differential scanning calorimetry, circular dicroism, tryptophan fluorescence, and size-exclusion chromatography. We show here that thermal unfolding of BSF occurs in two distinct steps corresponding to transitions from the native (N) to an intermediate (I) and from the intermediate to the unfolded...
متن کاملNative topology determines force-induced unfolding pathways in globular proteins.
Single-molecule manipulation techniques reveal that stretching unravels individually folded domains in the muscle protein titin and the extracellular matrix protein tenascin. These elastic proteins contain tandem repeats of folded domains with beta-sandwich architecture. Herein, we propose by stretching two model sequences (S1 and S2) with four-stranded beta-barrel topology that unfolding force...
متن کاملUsing nuclear magnetic resonance spectroscopy to study molten globule states of proteins.
Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique for the study of the structure, dynamics, and folding of proteins in solution. It is particularly powerful when applied to dynamic or flexible systems, such as partially folded molten globule states of proteins, which are not usually amenable to X-ray crystallography. In this article, NMR methods suitable for the detailed cha...
متن کاملDifferent subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin.
alpha-Lactalbumin (alpha-LA) is a two-domain, calcium-binding protein that forms one of the best studied molten globules. We present here amide hydrogen exchange studies of the molten globule formed by human alpha-LA at pH 2 and compare these results with a similar study of the native state at pH 6.3. The most persistent structure in the molten globule is localized in the helical domain, consis...
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ژورنال
عنوان ژورنال: Folding and Design
سال: 1996
ISSN: 1359-0278
DOI: 10.1016/s1359-0278(96)00020-x