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. In this study, we characterize in detail some of the physicochemical properties of partially denatured states of yeast glutathione reductase
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. The bacterially expressed protein (rSBA) has a molecular mass of 27,586 kDa and is devoid of covalently linked carbohydrates
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. It is also seen that fluctuations span the spectrum of shapes and sizes
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. Internal correlations show scale invariance As noted in the introduction, the self-repelling nature of proteins in the EV limit imposes correlations on all length scales
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. Processes that disrupt or uncouple this balance have the potential to alter normal cell turnover, ultimately resulting in the induction of lung pathology and disease
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. Am J Respir Crit Care Med 1997; 156:1969-1977(7) Hodge S, Hodge G, Holmes M, et al
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. 6-fold for C3A/C26A, 26-fold for I7S, and 30-fold for F110S
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. We anticipate that the observations made below for BSA apply equally to LDH, YADH, and LADH
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. Alternately, it is possible that multiple Gβ86-105 peptides bind to the enzyme giving the same overall volume change
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. Untangling of amyloid architecture and intrafibrillar packing of the β-pleated sheets is the key issue in designing inhibitors of the fibrillar growth-pharmaceuticals that could prevent spreading of a misfolded protein in diseased tissues (Cohen and Kelly, 2003)
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. As apparent from dynamic light scattering studies, the intermediate observed during unfolding of rSBA is monomeric in nature
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