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Intrinsic tryptophans of CRABPI as probes of structure and folding.
Site-specific fluorescent labeling of poly-histidine sequences using a metal-chelating cysteine.
Defining the structure of the substrate-free state of the DnaK molecular chaperone.
Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.
Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling.
Effect of charged residue substitutions on the membrane-interactive properties of signal sequences of the Escherichia coli LamB protein.
Effect of charged residue substitutions on the thermodynamics of signal peptide-lipid interactions for the Escherichia coli LamB signal sequence.
Aggregation of a slow-folding mutant of a beta-clam protein proceeds through a monomeric nucleus.
Fluorescence analysis of tryptophan-containing variants of the LamB signal sequence upon insertion into a lipid bilayer.
Conformational and membrane-binding properties of a signal sequence are largely unaltered by its adjacent mature region.
Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant.
A method for direct measurement of protein stability in vivo.
Using a low denaturant model to explore the conformational features of translocation-active SecA.
Effect of tryptophan derivatives on the phase properties of bilayers.