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The folding kinetics and thermodynamics of the FYN-SH3 domain
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Different folding transition states may result in the same native structure
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of outstanding interest. The crystal structures of two circular permutants of the SH3 domain of α-spectrin were solved, showing that they retained the wild-type structure. Mutant analysis, however, showed that the two permutants fold through different transition states.
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0031011695
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Reversible unfolding of individual titin immunoglobulin domains by AFM
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of outstanding interest. This paper, along with [29,30], describes studies that use the enormous power of single-molecule measurements to show that the elasticity of the muscle protein titin is due to the folding and unfolding of the all-β sheet fibronectin and immunoglobulin domains from which it is built.
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of outstanding interest Rief M, Gautel M, Oesterhelt F, Fernandez JM, Graub HE. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1997;1109-1112 This paper, along with [29,30], describes studies that use the enormous power of single-molecule measurements to show that the elasticity of the muscle protein titin is due to the folding and unfolding of the all-β sheet fibronectin and immunoglobulin domains from which it is built.
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of outstanding interest. See annotation [28].
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of outstanding interest Kellermayer MSZ, Smith SB, Granzier HL, Bustamante C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science. 276:1997;1112-1116 See annotation [28].
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Elasticity and unfolding of single molecules of the giant muscle protein titin
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of outstanding interest. See annotation [28].
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of outstanding interest Tskhovrebova L, Trinick J, Sleep JA, Simmons RM. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 387:1997;308-312 See annotation [28].
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Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: Evidence for hairpins as initiation sites for β-sheet formation
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of special interest. The m-value analysis of two mutants of tendamistat, each missing one of the two disulfide bonds present in the wild-type, suggests that the first hairpin of the protein is fully formed in the transition state and may initiate the folding of the protein.
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of special interest Schönbrunner N, Pappenberger G, Scharf M, Engels J, Kiefhaber T. Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding: evidence for hairpins as initiation sites for β-sheet formation. Biochemistry. 36:1997;9057-9065 The m-value analysis of two mutants of tendamistat, each missing one of the two disulfide bonds present in the wild-type, suggests that the first hairpin of the protein is fully formed in the transition state and may initiate the folding of the protein.
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A statistical analysis of various global folding parameters of proteins that fold by a two-state transition showed that the rate of folding and the α-value of the transition state are both related to the extent to which local interactions stabilize the native protein of special interest
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of special interest Plaxco KW, Simons KT, Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J Mol Biol. 1998; A statistical analysis of various global folding parameters of proteins that fold by a two-state transition showed that the rate of folding and the α-value of the transition state are both related to the extent to which local interactions stabilize the native protein.
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Baker, D.3
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Intrinsic tryptophans of CRABPI as probes of structure and folding
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Clark PL, Liu Z-P, Zhang J, Gierasch LM. Intrinsic tryptophans of CRABPI as probes of structure and folding. Protein Sci. 5:1996;1108-1117.
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Clark, P.L.1
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0030716169
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Cavity formation before stable hydrogen bonding in the folding of a β-clam protein
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of special interest. ANS binding (as a substrate mimic) and quench flow hydrogen exchange analysis of the folding of CRABPI was performed to demonstrate that the intermediate formed has a native like topology without a stable hydrogen bonding network.
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of special interest Clark PL, Liu Z-P, Rizo J, Gierasch LM. Cavity formation before stable hydrogen bonding in the folding of a β-clam protein. Nat Struct Biol. 4:1997;883-886 ANS binding (as a substrate mimic) and quench flow hydrogen exchange analysis of the folding of CRABPI was performed to demonstrate that the intermediate formed has a native like topology without a stable hydrogen bonding network.
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0031010678
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40
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0030871209
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Acquisition of native β-strand topology during the rapid collapse phase of protein folding
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of special interest. Competition hydrogen exchange experiments were carried out using a variety of pH values to show that weak hydrogen exchange protection is established over the entire molecule within the 1 ms dead-time of the experiment.
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of special interest Parker MJ, Dempsey C, Lorch M, Clarke AR. Acquisition of native β-strand topology during the rapid collapse phase of protein folding. Biochemistry. 36:1997;13396-13405 Competition hydrogen exchange experiments were carried out using a variety of pH values to show that weak hydrogen exchange protection is established over the entire molecule within the 1 ms dead-time of the experiment.
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41
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0031574916
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Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain
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of special interest. α-helical propensity was introduced into the 19 N-terminal residues of the SH3 domain from α-spectrin. It was shown that although these residues form a helical structure in the unfolded state they form a β-structure in the fully folded protein.
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of special interest Prieto J, Wilmans M, Jiménez MA, Rico M, Serrano L. Non-native local interactions in protein folding and stability: introducing a helical tendency in the all β-sheet α-spectrin SH3 domain. J Mol Biol. 268:1997;760-778 α-helical propensity was introduced into the 19 N-terminal residues of the SH3 domain from α-spectrin. It was shown that although these residues form a helical structure in the unfolded state they form a β-structure in the fully folded protein.
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0029740071
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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. Stopped flow circular dichroism experiments show that this predominantly β-sheet protein folds through an intermediate with a high α-helical content.
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of special interest Hamada D, Segawa S-I, Goto Y. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat Struct Biol. 3:1996;868-873 Stopped flow circular dichroism experiments show that this predominantly β-sheet protein folds through an intermediate with a high α-helical content.
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Consideration of the possibility that the slow step in protein denaturation is due to cis-trans isomerism of proline residues
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Evidence for an obligatory intermediate in the folding of interleukin-1β
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of outstanding interest. The folding transition of interleukin-1β was followed using quench flow hydrogen exchange in combination with ESI-MS, so the populations of the unfolded, intermediate and native states of the protein could be followed individually. Due to the slow formation of the intermediate, a lag in the rate of formation of the native state was detected, demonstrating that the intermediate formed is on the folding pathway.
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of outstanding interest Heidary DK, Gross LA, Roy M, Jennings PA. Evidence for an obligatory intermediate in the folding of interleukin-1β Nat Struct Biol. 4:1997;725-731 The folding transition of interleukin-1β was followed using quench flow hydrogen exchange in combination with ESI-MS, so the populations of the unfolded, intermediate and native states of the protein could be followed individually. Due to the slow formation of the intermediate, a lag in the rate of formation of the native state was detected, demonstrating that the intermediate formed is on the folding pathway.
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