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. Phase diagram for acidic conformational states of apomyoglobin
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. Instead, new local contacts would he added onto those that already exist in the denatured state
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. Fifty years of solvent denaturation
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. Conformational constraints for amyloid formation: the importance of being unfolded
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. A Gaussian-chain model for treating residual charge-charge interactions in the unfolded state of proteins
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. The high response of tetrameric proteins may suggest a particular destabilization of the native structure associated to the oligomeric state, a perturbation probably related to dissociation of the subunits and exposure of previously buried hydrophobic regions
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. In this case, however, stabilization of the native state is most probably due to a decrease in free energy of the native state; phosphate, like sulfate, is a salting-out ion that stabilizes folded protein structures and favors aggregation and precipitation
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. For many years in the physical chemistry of DNA there was no clear discrimination between processes that involved chemical binding with coil DNA molecules in solution and changes in the conformation of DNA such as compaction
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. One round of water rinsing was performed applying 5 µl water
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. In contrast, when there are packing voids, the stability of membrane binding of a protein under pressure will depend on its ability to deform under pressure to fill in voids and reduce the volume
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. The pleckstrin homology domain of phospholipase C-β^sub 2^ links the binding of Gβγ to the catalytic core
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. For if a residue contributes via nonnative interactions to the stable hypergutter that concludes the dominant (longest) diffusive search, then mutations to that residue will affect the folding rate, even though it does not necessarily possess any native contacts at the transition state
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. Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model
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. The high response of tetrameric proteins may suggest a particular destabilization of the native structure associated to the oligomeric state, a perturbation probably related to dissociation of the subunits and exposure of previously buried hydrophobic regions
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