Protein Folding: Solid evidence for molten globules
暂无分享,去创建一个
[1] P. S. Kim,et al. A protein dissection study of a molten globule. , 1994, Biochemistry.
[2] S. Radford,et al. Probing the structure of folding intermediates , 1994 .
[3] C M Dobson,et al. Understanding how proteins fold: the lysozyme story so far. , 1994, Trends in biochemical sciences.
[4] P E Wright,et al. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. , 1993, Science.
[5] D. Shortle,et al. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study. , 1994, Biochemistry.
[6] K. Wüthrich. NMR assignments as a basis for structural characterization of denatured states of globular proteins , 1994 .
[7] D. Shortle,et al. NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease. , 1993, Structure.
[8] Christopher M. Dobson,et al. Structural characterization of a highly–ordered ‘molten globule’ at low pH , 1994, Nature Structural Biology.
[9] Matthews Cr. PATHWAYS OF PROTEIN FOLDING , 1993 .
[10] C M Dobson,et al. Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study. , 1993, Biochemistry.
[11] T. Creighton,et al. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. , 1993, Journal of molecular biology.
[12] B. Stockman,et al. Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: The A-state of human ubiquitin , 1993, Journal of biomolecular NMR.
[13] C. Dobson,et al. A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding. , 1993, Biochemistry.
[14] T. Sosnick,et al. The barriers in protein folding , 1994, Nature Structural Biology.
[15] K. Dill,et al. Origins of structure in globular proteins. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[16] C. Levinthal. Are there pathways for protein folding , 1968 .
[17] F. Hartl,et al. Molecular chaperone functions of heat-shock proteins. , 1993, Annual review of biochemistry.
[18] H. Dyson,et al. Peptide conformation and protein folding , 1993 .
[19] J. Sambrook,et al. Protein folding in the cell , 1992, Nature.
[20] P. S. Kim,et al. Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor , 1990, Nature.
[21] Y. Thériault,et al. Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride. , 1994, Journal of molecular biology.
[22] G. Wider,et al. NMR determination of residual structure in a urea-denatured protein, the 434-repressor. , 1992, Science.
[23] Lila M. Gierasch,et al. Protein Folding: Deciphering the Second Half of the Genetic Code , 1990 .
[24] A. Joshua Wand,et al. Solution structure of apocytochrome b562 , 1994, Nature Structural Biology.