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. Being at the noncanonical interface, these glycans must be profoundly involved in holding the tetrameric structure rather than being involved in the folding of individual monomeric unit
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. (28) found by principal component analysis that gorge-opening behavior is not dominated by a few principal dynamical components but rather by a hierarchy of motions on different timescales acting together
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. Moreover, residues with significant exchange broadening are found
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. This indicates that the Bis-ANS molecule is too big to completely fit in the thyroxine binding cavity and likely there is only room for one-half of the symmetric molecule
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.3 mol of reactive SH group per mol of monomer under native conditions, indicating that one of the thiol groups of GR is partially accessible to DTNB in the folded protein
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. INTRODUCTION Most proteins are characterized by well-defined three-dimensional structures, which in general exist only within the limits of specific environmental conditions
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. The shape of the emission spectrum of pure L-tryptophan (see Fig
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. Assuming at least a qualitative relation between the absence of aggregation and larger red shifts for the unfolded states of BSUA, BLA, and BAA we can state the following: (1), the smallest heating rate (0
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. Denaturation of the native enzyme is reflected by a relative increase of MSDs consistent with entropic stabilization of the unfolded state
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. An important time window in the picosecond-to-nanosecond time range is occupied by atomic thermal fluctuations, which have been extensively investigated by molecular dynamics (MD) simulations (2), and by various experimental approaches including neutron scattering (3,4) and nuclear magnetic resonance (NMR) (5)
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. The spectra obtained upon direct excitation of ANS and Bis-ANS are shown in Fig
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. Dried lipids were suspended in 150mM NaCl, 20mM Hepes (pH 7
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. The CD data of the apoA-1-, apoA-2-, and apoC-1-containing disks recorded in a T-jump from 25 to 85°C indicate that the unfolding is slowest for apoA-1 and fastest for apoC-1 (Fig
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. 2) than those with apoA-1 (data not shown)
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. The insulin aggregation involves only noncovalent interactions, and the disulfide bridges do not undergo recombination during the process
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. This suggests a partition of the folding space into "rapid" dimensions representing the local formation of secondary structure, and "slow" dimensions representing the topomer search
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. Interpreting the folding kinetics of helical proteins
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