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0029967474
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Uversky VN, Ptitsyn OB. 'Partly folded' state, a new equilibrium of protein molecules: four-state guanidinium chloride-induce unfolding of β-lactamase at low temperature. Biochemistry. 33:1994;2782-2791.
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Further evidence on the equilibrium 'pre-molten globule state': Four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature
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of special interest. The GuHCI-induced unfolding transition of carbonic anhydrase monitored by spectroscopic and hydrodynamic probes exhibits two equilibrium intermediates. On the basis of its compactness, secondary structure and ANS binding properties, the less stable 'pre-molten globule state' is proposed to be an equilibrium analog of early kinetic intermediates.
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Uversky VN, Ptitsyn OB. Further evidence on the equilibrium 'pre-molten globule state': four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature. of special interest J Mol Biol. 255:1996;215-228 The GuHCI-induced unfolding transition of carbonic anhydrase monitored by spectroscopic and hydrodynamic probes exhibits two equilibrium intermediates. On the basis of its compactness, secondary structure and ANS binding properties, the less stable 'pre-molten globule state' is proposed to be an equilibrium analog of early kinetic intermediates.
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of special interest. The stable intermediate of apomyoglobin at pH4 is formed during an apparent two-state reaction that has rates in the millisecond time range. Although there is no detectable intermediate during refolding, a missing amplitude effect in unfolding experiments suggests formation of an early unfolding intermediate.
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Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
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of special interest. The structure and stability of the molten-globule intermediate of α-lactalbumin were probed by replacing exposed α-helical residues with prolines. Proline substitution caused individual helices to unfold without preventing association of the remaining helices, indicating that the molten globule of α-lactalbumim is formed in a noncooperative transition.
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Schulman BA, Kim PS. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. of special interest Nat Struct Biol. 3:1996;1-6 The structure and stability of the molten-globule intermediate of α-lactalbumin were probed by replacing exposed α-helical residues with prolines. Proline substitution caused individual helices to unfold without preventing association of the remaining helices, indicating that the molten globule of α-lactalbumim is formed in a noncooperative transition.
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of special interest. The kinetics of folding and unfolding of cyt c was studied at pH5, where the involvement of non-native heme ligands is minimized. Based on the behavior of fragments (residues 1-65 and 1-80), the authors describe the burst phase observed during folding as a solvent-dependent contraction of the polypeptide chain that makes no favorable contribution to the folding process.
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Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
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of special interest. The refolding kinetics of α-lactalbumin was investigated using stopped-flow CD, fluorescence techniques and pulsed hydrogen exchange. Formation of a burst intermediate with significant amounts of secondary structure was observed within the dead time of the experiment. The similarity of structure, stability, and solvent exposure of this intermediate and the equilibrium molten globule of α-lactalbumin suggests that they are closely related.
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Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
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of special interest. The stopped-flow CD analysis of the refolding kinetics of β-lactoglobulin reveals an accumulation of a non-native early folding intermediate containing significant amounts of α-helical structure.
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Hamada D, Segawa S-I, Goto Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. of special interest Nat Struct Biol. 3:1996;868-873 The stopped-flow CD analysis of the refolding kinetics of β-lactoglobulin reveals an accumulation of a non-native early folding intermediate containing significant amounts of α-helical structure.
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NMR determination of residual structure in a urea-denatured protein, the 434-repressor
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The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain - chain interactions by NMR and CD spectroscopy
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Wang Y, Shortle D. The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain - chain interactions by NMR and CD spectroscopy. Biochemistry. 34:1995;15895-15905.
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Microsecond protein folding through a compact transition state
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6-85, observed in the absence of denaturant, is 250 μs, and extrapolation of the kinetics for the refolding of Glu46→Ala/Glu48→Ala leads to an estimate of 20 μs.
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6-85, observed in the absence of denaturant, is 250 μs, and extrapolation of the kinetics for the refolding of Glu46→Ala/Glu48→Ala leads to an estimate of 20 μs.
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Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G
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Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition
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Viguera AR, Martinez JC, Filimonov VV, Mateo PL, Serrano L. Thermodynamic and kinetic analysis of the SH3 domain of spectrin shows a two-state folding transition. Biochemistry. 33:1994;2142-2150.
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Folding of a four-helix bundle: Studies of acyl-coenzyme A binding protein
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Kragelund BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM. Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. Biochemistry. 34:1995;7217-7224.
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Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
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Villegas V, Azuaga A, Catasus L, Raverter D, Mateo PL, Avilés FX, Serrano L. Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2. Biochemistry. 34:1995;15105-15110.
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Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
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of special interest. The refolding of dimeric Arc repressor was shown to become diffusion-controlled when three buried amino acids involved in salt bridge and hydrogen-bonding interactions were replaced by three hydrophobic residues. The kinetic effects of protein concentration, solvent viscosity and denaturant concentration are consistent with a three-state folding mechanism involving a loosely folded dimeric intermediate. Removal of the buried charges lowers the conformational barrier, resulting in a change in the rate-limiting step.
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Waldburger CD, Jonsson T, Sauer RT. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. of special interest Proc Natl Acad Sci USA. 93:1996;2629-2634 The refolding of dimeric Arc repressor was shown to become diffusion-controlled when three buried amino acids involved in salt bridge and hydrogen-bonding interactions were replaced by three hydrophobic residues. The kinetic effects of protein concentration, solvent viscosity and denaturant concentration are consistent with a three-state folding mechanism involving a loosely folded dimeric intermediate. Removal of the buried charges lowers the conformational barrier, resulting in a change in the rate-limiting step.
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West MW, Hecht MH. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Sci. 4:1995;2032-2039.
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Conformation of peptide fragments of proteins in solution: Implications for initiation of protein folding
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Wright PE, Dyson HJ, Lerner RA. Conformation of peptide fragments of proteins in solution: implications for initiation of protein folding. Biochemistry. 27:1988;7167-7175.
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Zhou HX, Hoess RH, DeGrado WF. In vitro evolution of thermodynamically stable turns. Nat Struct Biol. 3:1996;446-451.
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