Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe

@article{Semisotnov1991StudyOT,
  title={Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe},
  author={Gennady V. Semisotnov and N. A. Rodionova and O I Razgulyaev and Vladimir Nikolaevich Uversky and A F Gripas' and Rudolf Gilmanshin},
  journal={Biopolymers},
  year={1991},
  volume={31}
}
Binding of the hydrophobia fluorescent probe, 1‐anilino‐naphthalene‐8‐sulfonate (ANS), to synthetic polypeptides and proteins with a different structural organization has been studied. It has been shown that ANS has a much stronger affinity to the protein “molten globule” state, with a pronounced secondary structure and compactness, but without a tightly packed tertiary structure as compared with its affinity to the native and coil‐like proteins, or to coil‐like, α‐helical, or β‐structural… Expand
Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
TLDR
Even with stable partially folded states, the development of the fluorescence enhancements resulting from interactions with 8‐anilino‐1‐naphthalenesulfonate can be relatively slow and kinetically complex. Expand
Differences in the Pathways of Proteins Unfolding Induced by Urea and Guanidine Hydrochloride: Molten Globule State and Aggregates
TLDR
What was previously believed to be the molten globule state in the pathway of protein denaturation by GdnHCl, in reality, for some proteins represents the aggregates of partially folded molecules. Expand
Hydrophobic photolabeling as a new method for structural characterization of molten globule and related protein folding intermediates
TLDR
The data, like NMR data, indicate that in the MG state of α‐lactalbumin, the α‐domain has a greater degree of persistent structure than the β‐domain, however, unlike the NMR method, the photolabeling method is not limited by the size of the protein and can provide information on several new residues. Expand
Creatinase in its collapsed A state shows properties of a molten globule with dimeric quaternary structure.
TLDR
The acid-induced structural characteristics of a homodimer, creatinase from Pseudomonas putida, are described and it is shown that native-like subunit interactions are involved in the stabilization of the A state of the enzyme. Expand
‘All‐or‐none’ mechanism of the molten globule unfolding
The Gdm‐HCl‐induced unfolding of bovine carbonic anhydrase B and S. aureus β‐lactamase was studied at 4°C by a variety of methods. With the use of FPLC it has been shown that within the transitionExpand
Similar toxicity of the oligomeric molten globule state and the prefibrillar oligomers
TLDR
It is demonstrated that the oligomeric molten globule is as toxic as the prefibrillar aggregates obtained at acid pH or the higher order oligomers prepared at neutral pH. Expand
Characterization of Acid-Induced Partially Folded Conformation Resembling a Molten Globule State of Polygalacturonase from a Filamentous Fungus Tetracoccosporium sp.
TLDR
The data imply the presence of MG state of PG at low pH, suggesting the phenomenon of hydrophobic collapse model for folding and integration into cell membrane. Expand
From coiled coils to small globular proteins: Design of a native‐like three‐helix bundle
TLDR
The attainment of a unique, native‐like state was achieved through the introduction of: helix capping interactions; electrostatic interactions between partially exposed charged residues; and a diverse collection of apolar side chains within the hydrophobic core. Expand
An enzymatic molten globule: efficient coupling of folding and catalysis.
TLDR
The results support the suggestion that many modern enzymes might have evolved from molten globule precursors, insofar as their structural plasticity confers relaxed substrate specificity and/or catalytic promiscuity, molten globules may also be attractive starting points for the evolution of new catalysts in the laboratory. Expand
Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
Backgound: The molten globule state is an intermediate between the native and the fully unfolded states of globular proteins and is purported to be an obligatory on-pathway intermediate of proteinExpand
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TLDR
It was shown that kinetic intermediate states accumulating in folding process reveal a native‐like compactness and secondary structure but have a symmetrized average environment of aromatic side groups and no esterase activity. Expand
Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism
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Kinetic refolding reactions of ferricytochrome c and β‐lactoglobulin have been studied by stopped‐flow circular dichroism by monitoring rapid ellipticity changes of peptide backbone and side‐chain chromophores to suggest the rapid formation of a secondary structure framework in protein folding is a common property observed in a variety of globular proteins. Expand
An early immunoreactive folding intermediate of the tryptophan synthase β2 subunit is a ‘molten globule’
TLDR
These results show the accumulation of an early transient folding intermediate which has a pronounced secondary structure and a high affinity for ANS, and which appears to have all the characteristics of the ‘molten globule’ state. Expand
A folding model of α-lactalbumin deduced from the three-state denaturation mechanism
Abstract It has been shown that α-lactalbumin undergoes a three-state denaturation, involving a helical intermediate state, on treatment with guanidine hydrochloride. The unfolding of the protein andExpand
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TLDR
A multi-domain model is proposed for penicillinase in which the domains can separate without appreciable change in secondary structure, important in understanding the means by which the enzyme activity can be controlled, and corresponds to a kinetic pathway of folding. Expand
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TLDR
Evidence is presented that beta-lactamase is close to fully unfolded at low ionic strength at the extremes of pH and that the presence of salt causes a cooperative transition to a conformation with the properties of a molten globule, namely, a compact state with native-like secondary structure but disordered side chains (tertiary structure). Expand
Binding of naphthalene dyes to the N and A conformers of bovine α-lactalbumin
Abstract Contrary to earlier findings, monomeric native α-lactalbumin does bind naphthalene dyes such as ANS and TNS with marked enhancement of their fluorescence. Nanosecond decay measurementsExpand
‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains
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Protein folding: Hypotheses and experiments
The current state of the problem of protein folding is reviewed with special attention to the novel “molten globule” state of the protein molecule, intermediate between the native and unfoldedExpand
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