Increasing the thermostability of staphylococcal nuclease: implications for the origin of protein thermostability
Tài liệu tham khảo
Byrne, 1995, Energetic contribution of side-chain hydrogen bonding to the stability of staphylococcal nuclease, Biochemistry, 34, 13949, 10.1021/bi00042a029
1994, The CCP4 suite, Acta. Crystallog. sect. D, 50, 760, 10.1107/S0907444994003112
Eftink, 1991, Fluorescence and conformational stability studies of staphylococcus nuclease and its mutants, including the less stable nuclease-concanavalin A hybrids, Biochemistry, 30, 1193, 10.1021/bi00219a005
Green, 1992, Contributions of the polar, uncharged amino acids to the stability of staphylococcal nuclease, Biochemistry, 31, 5717, 10.1021/bi00140a005
Gromiha, 1999, ProTherm, Nucl. Acids Res., 27, 286, 10.1093/nar/27.1.286
Hurley, 1994, The role of interior side-chain packing in protein folding stability, 549
Hynes, 1991, The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution, Proteins: Struct. Funct. Genet., 10, 92, 10.1002/prot.340100203
Jaenicke, 1998, The stability of proteins in extreme environments, Curr. Opin. Struct. Biol., 8, 738, 10.1016/S0959-440X(98)80094-8
Karshikoff, 1998, Proteins from thermophilic and mesophilic organisms essentially do not differ in packing, Protein Eng., 11, 867, 10.1093/protein/11.10.867
Ladenstein, 1998, Proteins from hyperthermophiles, Advan. Biochem. Eng. Biotechnol., 61, 37
Lee, 2000, Theoretical studies of the response of a protein structure to cavity-creating mutations, Biophys. J., 78, 1665, 10.1016/S0006-3495(00)76718-X
Malakauskas, 1998, Design, structure and stability of a hyperthermophilic protein variant, Nature Struct. Biol., 5, 470, 10.1038/nsb0698-470
Pantoliano, 1989, Large increases in general stability for subtilisin BPN’ through incremental changes in the free energy of unfolding, Biochemistry, 28, 7205, 10.1021/bi00444a012
Querol, 1996, Analysis of protein conformational characteristics related to thermostability, Protein Eng., 9, 265, 10.1093/protein/9.3.265
Richards, 1997, Protein stability, Cell. Mol. Life Sci., 53, 790, 10.1007/s000180050100
Richards, 1993, An analysis of packing in the protein folding problem, Quart. Rev. Biophys., 26, 423, 10.1017/S0033583500002845
Salminen, 1996, An unusual route to thermostability disclosed by the comparison of Thermus thermophilus and Escherichia coli inorganic pyrophosphatases, Protein Sci., 5, 1014, 10.1002/pro.5560050604
Scandurra, 1998, Protein thermostability in extremophiles, Biochimie, 80, 933, 10.1016/S0300-9084(00)88890-2
Schwehm, 1998, Application of automated methods for determination of protein conformational stability, Methods Enzymol., 295, 150, 10.1016/S0076-6879(98)95039-X
Shortle, 1986, Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease, J. Cell Biochem., 30, 281, 10.1002/jcb.240300402
Stearman, 1988, Combining thermostable mutations increases the stability of lambda repressor, Biochemistry, 27, 7571, 10.1021/bi00419a059
Stites, 1995, Instrumentation for automated determination of protein stability, Anal. Biochem., 227, 112, 10.1006/abio.1995.1259
Szilagyi, 2000, Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits, Struct. Fold. Des., 8, 493, 10.1016/S0969-2126(00)00133-7
Usher, 1998, Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability, Protein Sci., 7, 403, 10.1002/pro.5560070221
Vlassi, 1999, A correlation between the loss of hydrophobic core packing interactions and protein stability, J. Mol. Biol., 285, 817, 10.1006/jmbi.1998.2342
Vogt, 1997, Protein thermal stability, Fold. Des., 2, S40, 10.1016/S1359-0278(97)00062-X
Vogt, 1997, Protein thermal stability, hydrogen bonds, and ion pairs, J. Mol. Biol., 269, 631, 10.1006/jmbi.1997.1042
Vriend, 1990, WHAT IF, J. Mol. Graph., 8, 52, 10.1016/0263-7855(90)80070-V
Wray, 1999, Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability, J. Mol. Biol., 292, 1111, 10.1006/jmbi.1999.3102
