Experimental investigation of sidechain interactions in early folding intermediates

Kim, 1990, Intermediates in the folding reactions of small proteins, Annu. Rev. Biochem, 59, 631, 10.1146/annurev.bi.59.070190.003215 Dill, 1993, Cooperativity in protein-folding kinetics, Proc. Natl Acad. Sci. U.S.A, 90, 1942, 10.1073/pnas.90.5.1942 Fersht, 1992, Pathway of protein folding, Faraday Discuss, 93, 183, 10.1039/fd9929300183 Englander, 1992, Protein folding studied using hydrogen-exchange labelling and two-dimensional NMR, Annu. Rev. Biophys. Biomol. Struct, 21, 243, 10.1146/annurev.bb.21.060192.001331 Chaffotte, 1992, Kinetic resolution of peptide bond and sidechain far-UV circular dichroism during the folding of hen egg white lysozyme, Biochemistry, 31, 9694, 10.1021/bi00155a024 Kuwajima, 1991, Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy, Biochemistry, 30, 7693, 10.1021/bi00245a005 Itzhaki, 1994, Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes, Biochemistry, 33, 5212, 10.1021/bi00183a026 Khorasanizadeh, 1993, Folding and stability of a tryptophan-containing mutant of ubiquitin, Biochemistry, 32, 7054, 10.1021/bi00078a034 Eftink, 1991, Fluorescence techniques for studying protein structure, Methods Biochem. Anal, 35, 127, 10.1002/9780470110560.ch3 Garvey, 1989, A hydrophobic cluster forms early in the folding of dihydrofolate reductase, Proteins, 6, 259, 10.1002/prot.340060308 Smith, 1991, Detection and characterization of intermediates in the folding of large proteins by the use of genetically inserted tryptophan probes, Biochemistry, 30, 1028, 10.1021/bi00218a021 Radford, 1992, The folding of hen lysozyme involves partially structured intermediates and multiple pathways, Nature, 358, 302, 10.1038/358302a0 Ballery, 1993, Characterization of an intermediate in the folding pathway of phosphoglycerate kinase —  chemical reactivity of genetically introduced cysteinyl residues during the folding process, Biochemistry, 32, 708, 10.1021/bi00053a040 Svensson, 1995, Mapping the folding intermediate of human carbonic anhydrase II: probing substructure by chemical reactivity and spin and fluorescence labelling of engineered cysteine residues, Biochemistry, 34, 8606, 10.1021/bi00027a010 Jones, 1995, Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy, Biochemistry, 34, 1867, 10.1021/bi00006a007 Semisotnov, 1987, Sequential mechanism of refolding of carbonic anhydrase B, FEBS Lett, 224, 9, 10.1016/0014-5793(87)80412-X Jennings, 1993, Reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four channel model, Biochemistry, 32, 3783, 10.1021/bi00065a034 Kuwajima, 1989, Characterization of the critical state in protein folding —  effects of guanidine-hydrochloride and specific Ca2+ binding on the folding kinetics of alpha-lactalbumin, J. Mol. Biol, 206, 547, 10.1016/0022-2836(89)90500-7 Jones, 1994, Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding, Biochemistry, 33, 15250, 10.1021/bi00255a005 Semisotnov, 1991, Study of the “molten globule” intermediate state in protein folding by a hydrophobic fluorescent probe, Biopolymers, 31, 119, 10.1002/bip.360310111 Engelhard, 1995, Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates, Protein Sci, 4, 1553, 10.1002/pro.5560040813 Ptitsyn, 1990, Evidence for a molten globule state as a general intermediate in protein folding, FEBS Lett, 262, 20, 10.1016/0014-5793(90)80143-7 Lattman, 1994, Small angle scattering studies of protein folding, Curr. Opin. Struct. Biol, 4, 87, 10.1016/S0959-440X(94)90064-7 Feng, 1995, Kinetics of compaction during lysozyme refolding studied by continuous-flow quasielastic light scattering, Biochemistry, 33, 13382, 10.1021/bi00249a026 Frieden, 1993, NMR and protein folding: equilibrium and stopped-flow studies, Protein Sci, 2, 2007, 10.1002/pro.5560021202 Balbach, 1995, Following protein-folding in real-time using NMR-spectroscopy, Nature Struct. Biol, 2, 865, 10.1038/nsb1095-865 Creighton, 1992, Protein folding pathways determined using disulphide bonds, Bioessays, 14, 195, 10.1002/bies.950140310 Van Mierlo, 1993, Partially folded conformation of the (30–51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor, J. Mol. Biol, 229, 1125, 10.1006/jmbi.1993.1108 Kawata, 1991, Use of fluorescence energy transfer to characterise the compactness of the constant fragment of an immunoglobulin light chain in the early stage of folding, Biochemistry, 30, 4367, 10.1021/bi00232a001 Amir, 1992, Detection of local structures in reduced unfolded bovine pancreatic trypsin-inhibitor, Proteins, 13, 162, 10.1002/prot.340130210 Matouschek, 1992, The folding of an enzyme IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure, J. Mol. Biol, 224, 819, 10.1016/0022-2836(92)90564-Z Horovitz, 1990, Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins, J. Mol. Biol, 214, 613, 10.1016/0022-2836(90)90275-Q