Simulation of the thermal denaturation of hen egg white lysozyme: trapping the molten globule state.
暂无分享,去创建一个
[1] T. Creighton,et al. The molten globule protein conformation probed by disulphide bonds , 1991, Nature.
[2] W. Kabsch,et al. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features , 1983, Biopolymers.
[3] C M Dobson,et al. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin. , 1989, Biochemistry.
[4] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.
[5] M. Karplus,et al. The hinge-bending mode in lysozyme , 1976, Nature.
[6] SRLSQ refinement of triclinic lysozyme , 1987 .
[7] A Ikai,et al. Kinetics of unfolding and refolding of proteins. 3. Results for lysozyme. , 1973, Journal of molecular biology.
[8] Sophianopoulos Aj,et al. THERMODYNAMICS OF CONFORMATIONAL CHANGES OF PROTEINS. I. PH-DEPENDENT DENATURATION OF MURAMIDASE. , 1964 .
[9] Christopher M. Dobson,et al. Demonstration by NMR of folding domains in lysozyme , 1991, Nature.
[10] H. Berendsen,et al. COMPUTER-SIMULATION OF MOLECULAR-DYNAMICS - METHODOLOGY, APPLICATIONS, AND PERSPECTIVES IN CHEMISTRY , 1990 .
[11] G. Ciccotti,et al. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes , 1977 .
[12] O. Ptitsyn,et al. Evidence for a molten globule state as a general intermediate in protein folding , 1990, FEBS letters.
[13] H. Berendsen,et al. Molecular dynamics with coupling to an external bath , 1984 .
[14] Andreas Matouschek,et al. Transient folding intermediates characterized by protein engineering , 1990, Nature.
[15] K. Kuwajima,et al. Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin. , 1985, Biochemistry.
[16] P. S. Kim,et al. Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.