Is protein folding hierarchic? II. Folding intermediates and transition states.
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[1] C. Tanford,et al. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. , 1971, The Journal of biological chemistry.
[2] H. Blaschek,et al. A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A. , 2005, European journal of biochemistry.
[3] E. Kaiser,et al. Amphiphilic secondary structure: design of peptide hormones. , 1984, Science.
[4] K. Kuwajima,et al. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme. , 1986, Biochemistry.
[5] S Sugai,et al. Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroism , 1987, FEBS letters.
[6] S. Walter Englander,et al. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR , 1988, Nature.
[7] P E Wright,et al. Structural characterization of a partly folded apomyoglobin intermediate. , 1990, Science.
[8] S W Englander,et al. Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. , 1990, Biochemistry.
[9] P E Wright,et al. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. , 1993, Science.
[10] J. King,et al. Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro. , 1993, The Journal of biological chemistry.
[11] L. H. Bradley,et al. Protein design by binary patterning of polar and nonpolar amino acids. , 1993, Methods in molecular biology.
[12] P. S. Kim,et al. A protein dissection study of a molten globule. , 1994, Biochemistry.
[13] R. Sauer,et al. P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refolding. , 1995, Biochemistry.
[14] J. Onuchic,et al. Funnels, pathways, and the energy landscape of protein folding: A synthesis , 1994, Proteins.
[15] A. Fersht,et al. The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. , 1995, Journal of molecular biology.
[16] Luis Serrano,et al. Different folding transition states may result in the same native structure , 1996, Nature Structural Biology.
[17] D. Hamada,et al. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein , 1996, Nature Structural Biology.
[18] H. Roder,et al. Kinetic intermediates in the formation of the cytochrome c molten globule , 1996, Nature Structural Biology.
[19] Michael S. Kay,et al. Packing interactions in the apomyglobin folding intermediate , 1996, Nature Structural Biology.
[20] Joachim Engels,et al. Native-like β-structure in a Trifluoroethanol-induced Partially Folded State of the All-β-sheet Protein Tendamistat , 1996 .
[21] P. S. Kim,et al. Context-dependent secondary structure formation of a designed protein sequence , 1996, Nature.
[22] M Karplus,et al. "New view" of protein folding reconciled with the old through multiple unfolding simulations. , 1997, Science.
[23] S. Marqusee,et al. Touring the landscapes: partially folded proteins examined by hydrogen exchange. , 1997, Structure.
[24] T. Kiefhaber,et al. Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediate. , 1997, Journal of Molecular Biology.
[25] Christopher M. Dobson,et al. A residue-specific NMR view of the non-cooperative unfolding of a molten globule , 1997, Nature Structural Biology.
[26] J. Udgaonkar,et al. Multiple intermediates and transition states during protein unfolding , 1997, Nature Structural Biology.
[27] K. Dill,et al. From Levinthal to pathways to funnels , 1997, Nature Structural Biology.
[28] V. Muñoz,et al. Folding dynamics and mechanism of β-hairpin formation , 1997, Nature.
[29] Suganthi Balasubramanian,et al. Protein alchemy: Changing β-sheet into α-helix , 1997, Nature Structural Biology.
[30] Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations , 1997, Nature Structural Biology.
[31] A. Fersht,et al. Folding intermediates of wild-type and mutants of barnase. I. Use of phi-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium. , 1998, Journal of molecular biology.
[32] Single-tryptophan mutants of monomeric tryptophan repressor: optical spectroscopy reveals nonnative structure in a model for an early folding intermediate. , 1998, Biochemistry.
[33] P. S. Kim,et al. A specific hydrophobic core in the alpha-lactalbumin molten globule. , 1998, Journal of molecular biology.
[34] A. Fersht,et al. The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for folding. , 1998, Journal of molecular biology.
[35] G. Pielak,et al. Native tertiary structure in an A-state. , 1998, Journal of molecular biology.
[36] D. Rousseau,et al. Folding intermediates in cytochrome c , 1998, Nature Structural Biology.
[37] David Baker,et al. Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain , 1998, Nature Structural &Molecular Biology.
[38] L. Serrano,et al. Obligatory steps in protein folding and the conformational diversity of the transition state , 1998, Nature Structural &Molecular Biology.
[39] H. Jane Dyson,et al. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding , 1998, Nature Structural Biology.
[40] V. Pande,et al. Pathways for protein folding: is a new view needed? , 1998, Current opinion in structural biology.
[41] G. Rose,et al. Is protein folding hierarchic? I. Local structure and peptide folding. , 1999, Trends in biochemical sciences.