$\require{mediawiki-texvc}$

연합인증

연합인증 가입 기관의 연구자들은 소속기관의 인증정보(ID와 암호)를 이용해 다른 대학, 연구기관, 서비스 공급자의 다양한 온라인 자원과 연구 데이터를 이용할 수 있습니다.

이는 여행자가 자국에서 발행 받은 여권으로 세계 각국을 자유롭게 여행할 수 있는 것과 같습니다.

연합인증으로 이용이 가능한 서비스는 NTIS, DataON, Edison, Kafe, Webinar 등이 있습니다.

한번의 인증절차만으로 연합인증 가입 서비스에 추가 로그인 없이 이용이 가능합니다.

다만, 연합인증을 위해서는 최초 1회만 인증 절차가 필요합니다. (회원이 아닐 경우 회원 가입이 필요합니다.)

연합인증 절차는 다음과 같습니다.

최초이용시에는
ScienceON에 로그인 → 연합인증 서비스 접속 → 로그인 (본인 확인 또는 회원가입) → 서비스 이용

그 이후에는
ScienceON 로그인 → 연합인증 서비스 접속 → 서비스 이용

연합인증을 활용하시면 KISTI가 제공하는 다양한 서비스를 편리하게 이용하실 수 있습니다.

Timeline: Protein engineering 20 years on

Nature reviews. Molecular cell biology, v.3 no.12, 2002년, pp.964 - 970  

Brannigan, James A. (James A. Brannigan and Anthony J. Wilkinson are at the Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, UK.) ,  Wilkinson, Anthony J. (James A. Brannigan and Anthony J. Wilkinson are at the Structural Biology Laboratory, Department of Chemistry, University of York, York YO10 5YW, UK.)

Abstract AI-Helper 아이콘AI-Helper

It is 20 years since site-directed mutagenesis was first used to modify the active site of an enzyme of known structure and mechanism. Since then, this method has contributed far-reaching insights into catalysis, specificity, stability and folding of proteins. Engineered proteins are now being used ...

참고문헌 (88)

  1. Acc. Chem. Res. JR Knowles 10 105 1977 10.1021/ar50112a001 Knowles, J. R. & Albery, W. J. Perfection in enzyme catalysis: the energetics of triose phosphate isomerase. Acc. Chem. Res. 10, 105-111 (1977). 

  2. AR Fersht 1977 Enzyme Structure and Mechanism Fersht, A. R. Enzyme Structure and Mechanism (W. H. Freeman & Co., San Francisco, 1977). 

  3. Nature Rev. Mol. Cell Biol. ID Campbell 3 377 2002 10.1038/nrm800 Campbell, I. D. The march of structural biology. Nature Rev. Mol. Cell Biol. 3, 377-381 (2002). 

  4. Nature G Winter 299 756 1982 10.1038/299756a0 Winter, G., Fersht, A. R., Wilkinson, A. J., Zoller, M. & Smith, M. Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding. Nature 299, 756-758 (1982). 

  5. Proc. Natl Acad. Sci. USA G Dalbadie-MacFarland 79 6409 1982 10.1073/pnas.79.21.6409 Dalbadie-MacFarland, G. et al. Oligonucleotide-directed mutagenesis as a powerful method for studies of protein function. Proc. Natl Acad. Sci. USA 79, 6409-6413 (1982). 

  6. Proc. Natl Acad. Sci. USA IS Sigal 79 7157 1982 10.1073/pnas.79.23.7157 Sigal, I. S., Harwood, B. G. & Arentzen, R. Thiol β-lactamase: replacement of the active site serine of RTEM β-lactamase by a cysteine residue. Proc. Natl Acad. Sci. USA 79, 7157-7160 (1982). 

  7. Nature PT Jones 321 522 1986 10.1038/321522a0 Jones, P. T., Dear, P. H., Foote, J., Neuberger, M. S. & Winter, G. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321, 522-525 (1986). 

  8. Nature MS Neuberger 312 604 1984 10.1038/312604a0 Neuberger, M. S., Williams, G. T. & Fox, R. O. Recombinant antibodies possessing novel effector functions. Nature 312, 604-608 (1984). 

  9. Biochemistry AJ Wilkinson 22 3581 1983 10.1021/bi00284a007 Wilkinson, A. J., Fersht, A. R., Blow, D. M. & Winter, G. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry 22, 3581-3586 (1983). 

  10. Proc. Natl Acad. Sci. USA RJ Leatherbarrow 82 7840 1985 10.1073/pnas.82.23.7840 Leatherbarrow, R. J., Fersht, A. R. & Winter, G. Transition-state stabilisation in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering. Proc. Natl Acad. Sci. USA 82, 7840-7844 (1985). 

  11. Nature AJ Wilkinson 307 187 1984 10.1038/307187a0 Wilkinson, A. J., Fersht, A. R., Blow, D. M., Carter, P. & Winter, G. A large increase in enzyme-substrate affinity by protein engineering. Nature 307, 187-188 (1984). 

  12. Nature AR Fersht 314 235 1985 10.1038/314235a0 Fersht, A. R. et al. Hydrogen bonding and biological specificity analysed by protein engineering. Nature 314, 235-238 (1985). 

  13. Annu. Rev. Genet. M Smith 19 423 1985 10.1146/annurev.ge.19.120185.002231 Smith, M. In vitro. mutagenesis. Annu. Rev. Genet. 19, 423-462 (1985). 

  14. Nature P Carter 332 564 1988 10.1038/332564a0 Carter, P. & Wells, J. A. Dissecting the catalytic triad of a serine protease. Nature 332, 564-568 (1988). 

  15. Phil. Trans. R. Soc. Lond. A JA Wells 317 415 1986 10.1098/rsta.1986.0051 Wells, J. A., Cunningham, B. C., Graycar, T. P. & Estell, D. A. Importance of hydrogen-bond formation in stabilizing the transition state of subtilisin. Phil. Trans. R. Soc. Lond. A 317, 415-423 (1986). 

  16. Proc. Natl Acad. Sci. USA P Bryan 83 3743 1986 10.1073/pnas.83.11.3743 Bryan, P., Pantoliano, M. W., Quill, S. G., Hsiao, H. -Y. & Poulos, T. Site-directed mutagenesis and the role of the oxyanion hole in subtilisin. Proc. Natl Acad. Sci. USA 83, 3743-3745 (1986). 

  17. J. Biol. Chem. BA Springer 264 3057 1989 10.1016/S0021-9258(18)94029-9 Springer, B. A. et al. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. J. Biol. Chem. 264, 3057-3060 (1989). 

  18. Nature SJ Gardell 317 551 1985 10.1038/317551a0 Gardell, S. J., Craik, C. S., Hilvert, D., Urdea, M. S. & Rutter, W. J. Site-directed mutagenesis shows that tyrosine 248 of carboxypeptidase A does not play a crucial role in catalysis. Nature 317, 551-555 (1985). 

  19. Nature CCF Blake 206 757 1965 10.1038/206757a0 Blake, C. C. F. et al. Structure of hen egg white lysozyme. A three-dimensional fourier synthesis at 2Å resolution. Nature 206, 757-763 (1965). 

  20. Nature DJ Vocadlo 412 835 2001 10.1038/35090602 Vocadlo, D. J., Davies, G. J., Laine, R. & Withers, S. G. Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412, 835-838 (2001). 

  21. Science ER Kantrowitz 241 669 1988 10.1126/science.3041592 Kantrowitz, E. R. & Lipscomb, W. N. Escherichia coli. aspartate transcarbamylase: the relation between structure and function. Science 241, 669-674 (1988). 

  22. Nature A Matouschek 340 122 1989 10.1038/340122a0 Matouschek, A., Kellis J. T. Jr, Serrano, L. & Fersht, A. R. Mapping the transition state and pathway of protein folding by protein engineering. Nature 340, 122-126 (1989). 

  23. Cell AR Fersht 108 573 2002 10.1016/S0092-8674(02)00620-7 Fersht, A. R. & Daggett, V. Protein folding and unfolding at atomic resolution. Cell 108, 573-582 (2002). 

  24. Biochemistry BW Matthews 26 6855 1987 10.1021/bi00396a001 Matthews, B. W. Genetic and structural analysis of the protein stability problem. Biochemistry 26, 6855-6888 (1987). 

  25. J. Biol. Chem. D Shortle 264 5315 1989 10.1016/S0021-9258(18)83544-X Shortle, D. Probing the determinants of protein folding and stability with amino acid substitutions. J. Biol. Chem. 264, 5315-5318 (1989). 

  26. Trends Biotechnol. FH Arnold 8 244 1990 10.1016/0167-7799(90)90186-2 Arnold, F. H. Engineering enzymes for non-aqueous solvents. Trends Biotechnol. 8, 244-249 (1990). 

  27. Science LJ Perry 226 555 1984 10.1126/science.6387910 Perry, L. J. & Wetzel, R. Disulfide bond engineering into T4 lysozyme: stabilization of the protein toward thermal inactivation. Science 226, 555-557 (1984). 

  28. Proc. Natl Acad. Sci. USA B Van den Burg 95 2056 1998 10.1073/pnas.95.5.2056 Van den Burg, B., Vriend, G., Veltman, O. R., Venema, G. & Eijsink, V. G. H. Engineering an enzyme to resist boiling. Proc. Natl Acad. Sci. USA 95, 2056-2060 (1998). 

  29. Nature AJ Russell 328 496 1987 10.1038/328496a0 Russell, A. J. & Fersht, A. R. Rational modification of enzyme catalysis by engineering surface charge. Nature 328, 496-500 (1987). 

  30. Biochemistry AR Fersht 26 6030 1987 10.1021/bi00393a013 Fersht, A. R., Leatherbarrow, R. J. & Wells, T. N. C. Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships. Biochemistry 26, 6030-6038 (1987). 

  31. Biochemistry JA Wells 29 8509 1990 10.1021/bi00489a001 Wells, J. A. Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517 (1990). 

  32. Science HM Wilks 242 1541 1988 10.1126/science.3201242 Wilks, H. M. et al. A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework. Science 242, 1541-1544 (1988). 

  33. Biochemistry HM Wilks 29 8587 1990 10.1021/bi00489a013 Wilks, H. M. et al. Designs for a broad substrate specificity keto acid dehydrogenase. Biochemistry 29, 8587-8591 (1990) 

  34. Biochemistry HM Wilks 31 7802 1992 10.1021/bi00149a009 Wilks, H. M. et al. Design of a specific phenyllactate dehydrogenase by peptide loop exchange on the Bacillus stearothermophilus lactate dehydrogenase framework. Biochemistry 31, 7802-7806 (1992). 

  35. Biochemistry L Graf 26 2616 1987 10.1021/bi00383a031 Graf, L. et al. Selective alteration of substrate specificity by replacement of aspartic acid-189 with lysine in the binding pocket of trypsin. Biochemistry 26, 2616-2623 (1987). 

  36. Biochemistry JJ Perona 34 1489 1995 10.1021/bi00005a004 Perona, J. J. et al. Structural origins of substrate discrimination in trypsin and chymotrypsin. Biochemistry 34, 1489-1499 (1995). 

  37. FEBS Lett. I Venekei 379 143 1996 10.1016/0014-5793(95)01484-5 Venekei, I., Szilagyi, L., Graf, L. & Rutter, W. J. Attempts to convert chymotrypsin to trypsin. FEBS Lett. 379, 143-147 (1996). 

  38. Nature H Bedouelle 320 371 1986 10.1038/320371a0 Bedouelle, H. & Winter, G. A model of synthetase/transfer RNA interaction as deduced by protein engineering. Nature 320, 371-373 (1986). 

  39. Science BC Cunningham 244 1081 1989 10.1126/science.2471267 Cunningham, B. C. & Wells, J. A. High-resolution epitope mapping of HGH-receptor interactions by alanine-scanning mutagenesis. Science 244, 1081-1085 (1989). 

  40. Trends Biochem. Sci. JA Wells 13 291 1988 10.1016/0968-0004(88)90121-1 Wells, J. A. & Estell, D. A. Subtilisin - an enzyme designed to be engineered. Trends Biochem. Sci. 13, 291-297 (1988). 

  41. Nature AR Duncan 332 738 1988 10.1038/332738a0 Duncan, A. R. & Winter, G. The binding site for C1q on IgG. Nature 332, 738-740 (1988). 

  42. Proc. Natl Aad. Sci. USA AR Oliphant 86 9094 1989 10.1073/pnas.86.23.9094 Oliphant, A. R. & Struhl, K. An efficient method for generating proteins with altered enzymatic properties: application to β-lactamase. Proc. Natl Aad. Sci. USA 86, 9094-9098 (1989). 

  43. Nature DD Loeb 340 397 1989 10.1038/340397a0 Loeb, D. D. et al. Complete mutagenesis of the HIV-1 protease. Nature 340, 397-400 (1989). 

  44. Biotechniques E Merino 12 508 1992 Merino, E., Osuna, J., Bolivar, F. & Soberon, X. A general, PCR-based method for single or combinatorial oligonucleotide-directed mutagenesis on pUC/M13 vectors. Biotechniques 12, 508-510 (1992). 

  45. R Dawkins 1986 The Blind Watchmaker: Why the Evidence of Evolution Reveals a Universe Without Design Dawkins, R. The Blind Watchmaker: Why the Evidence of Evolution Reveals a Universe Without Design (Longman, London, 1986). 

  46. Proc. Natl Acad. Sci. USA K Chen 90 5618 1993 10.1073/pnas.90.12.5618 Chen, K. & Arnold, F. H. Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc. Natl Acad. Sci. USA 90, 5618-5622 (1993). 

  47. Nature G Winter 349 293 1991 10.1038/349293a0 Winter, G. & Milstein, C. Man-made antibodies. Nature 349, 293-299 (1991). 

  48. Nature WP Stemmer 370 389 1994 10.1038/370389a0 Stemmer, W. P. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370, 389-391 (1994). 

  49. Nature A Crameri 391 288 1998 10.1038/34663 Crameri, A., Raillard, S. A., Bermudez, E. & Stemmer, W. P. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391, 288-291 (1998). 

  50. Acc. Chem. Res. FH Arnold 31 125 1998 10.1021/ar960017f Arnold, F. H. Design by directed evolution. Acc. Chem. Res. 31, 125-131 (1998). 

  51. Proc. Natl Acad. Sci USA WPC Stemmer 91 10747 1994 10.1073/pnas.91.22.10747 Stemmer, W. P. C. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl Acad. Sci USA 91, 10747-10751 (1994). 

  52. J. Mol. Evol. K Miyazaki 49 716 1999 10.1007/PL00006593 Miyazaki, K. & Arnold, F. H. Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J. Mol. Evol. 49, 716-720 (1999). 

  53. Nucleic Acids Res. P Gaytan 30 e84 2002 10.1093/nar/gnf083 Gaytan, P., Osuna, J. & Soberon, X. Novel ceftazidime-resistance β-lactamases generated by a codon-based mutagenesis method and selection. Nucleic Acids Res. 30, e84 (2002). 

  54. Nature Biotechnol. H Murakami 20 76 2002 10.1038/nbt0102-76 Murakami, H., Hohsaka, T. & Sisido, M. Random insertion and deletion of arbitrary number of bases for codon-based random mutation of DNAs. Nature Biotechnol. 20, 76-81 (2002). 

  55. Proc. Natl Acad. Sci. USA G Xia 99 6597 2002 10.1073/pnas.102577799 Xia, G., Chen, L., Sera, T., Fa, M., Schultz, P. G. & Romesberg, F. E. Directed evolution of novel polymerase activities: mutation of a DNA polymerase into an efficient RNA polymerase. Proc. Natl Acad. Sci. USA 99, 6597-6602 (2002). 

  56. Curr. Opin. Biotechnol. AD Griffiths 11 338 2000 10.1016/S0958-1669(00)00109-9 Griffiths, A. D. & Tawfik, D. S. Man-made enzymes - from design to in vitro compartmentalisation. Curr. Opin. Biotechnol. 11, 338-353 (2000). 

  57. Proc. Natl Acad. Sci. USA FJ Ghadessy 98 4552 2001 10.1073/pnas.071052198 Ghadessy, F. J., Ong, J. L. & Holliger, P. Directed evolution of polymerase function by compartmentalised self-replication. Proc. Natl Acad. Sci. USA 98, 4552-4557 (2001). 

  58. Nature Biotechnol. MT Facciotti 17 593 1999 10.1038/9909 Facciotti, M. T., Bertain, P. B. & Yuan, L. Improved stearate phenotype in transgenic canola expressing a modified acyl-acyl carrier protein thioesterase. Nature Biotechnol. 17, 593-597 (1999). 

  59. Protein Eng. M Lehmann 15 403 2002 10.1093/protein/15.5.403 Lehmann, M. et al. The consensus concept for thermostability engineering of proteins: further proof of concept. Protein Eng. 15, 403-411 (2002). 

  60. Nature Biotechnol. SG Burton 20 37 2002 10.1038/nbt0102-37 Burton, S. G. The search for the ideal biocatalyst. Nature Biotechnol. 20, 37-45 (2002). 

  61. Nature Biotechnol. T Kumamaru 16 663 1998 10.1038/nbt0798-663 Kumamaru, T., Suenaga, H., Mitsuoka, M., Watanabe, T. & Furukawa, K. Enhanced degradation of polychlorinated biphenyls by directed evolution of biphenyl oxygenase. Nature Biotechnol. 16, 663-666 (1998). 

  62. Nature H Bayley 413 226 2001 10.1038/35093038 Bayley, H. & Cremer, P. S. Stochastic sensors inspired by biology. Nature 413, 226-230 (2001). 

  63. Cancer Metastasis Rev. P Holliger 18 411 1999 10.1023/A:1006314421941 Holliger P. & Bohlen, H. Engineering antibodies for the clinic. Cancer Metastasis Rev. 18, 411-419 (1999). 

  64. Curr. Opin. Struct. Biol. J McCafferty 10 417 2000 10.1016/S0959-440X(00)00108-1 McCafferty, J. & Glover, D. R. Engineering therapeutic proteins. Curr. Opin. Struct. Biol. 10, 417-420 (2000). 

  65. Br. J. Haematol. RM Winslow 111 387 2000 10.1046/j.1365-2141.2000.02326.x Winslow, R. M. Blood substitutes: refocusing an elusive goal. Br. J. Haematol. 111, 387-396 (2000). 

  66. Nature MF Perutz 228 726 1970 10.1038/228726a0 Perutz, M. F. Stereochemistry of the cooperative effects in haemoglobin. Nature 228, 726-734 (1970). 

  67. RE Dickerson 1983 Haemoglobin: Structure, Function, Evolution and Pathology Dickerson, R. E. & Geis, I. Haemoglobin: Structure, Function, Evolution and Pathology (Benjamin/Cummings Publishing Co., Inc., Menlo Park, California, 1983). 

  68. Nature D Looker 356 258 1992 10.1038/356258a0 Looker, D. et al. A human recombinant haemoglobin designed for use as a blood substitute. Nature 356, 258-260 (1992). 

  69. Artif. Cells Blood Substit. Immobil. Biotechnol. J,S Olson 25 227 1997 10.3109/10731199709118912 Olson, J, S., Eich, R., Smith, L. P., Warren, J. J. & Knowles, B. C. Protein engineering strategies for designing more stable hemoglobin-based blood substitutes. Artif. Cells Blood Substit. Immobil. Biotechnol. 25, 227-241 (1997). 

  70. Nature Biotechnol. DH Doherty 16 672 1998 10.1038/nbt0798-672 Doherty, D. H. et al. Rate of reaction with nitric oxide determines the hypertensive effect of cell-free hemoglobin. Nature Biotechnol. 16, 672-676 (1998). 

  71. Adv. Drug Deliv. Rev. J Brange 35 307 1999 10.1016/S0169-409X(98)00079-9 Brange, J. & Vølund, A. Insulin analogs with improved pharmacokinetic profiles. Adv. Drug Deliv. Rev. 35, 307-335 (1999). 

  72. Pharmacol. Rev. Z Vajo 52 1 2000 Vajo, Z. & Duckworth, W. C. Genetically engineered insulin analogues: diabetes in the new millennium. Pharmacol. Rev. 52, 1-10 (2000). 

  73. Adv. Protein Chem. T Blundell 26 279 1972 10.1016/S0065-3233(08)60143-6 Blundell, T., Dodson, G., Hodgkin, D. & Mercola, D. Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv. Protein Chem. 26, 279-402 (1972). 

  74. Nature J Brange 333 679 1988 10.1038/333679a0 Brange, J. et al. Monomeric insulins obtained by protein engineering and their medical implications. Nature 333, 679-682 (1988). 

  75. Science JR Knowles 236 1252 1987 10.1126/science.3296192 Knowles, J. R. Tinkering with enzymes: What are we learning. Science 236, 1252-1259 (1987). 

  76. Proc. Natl Acad. Sci. USA T Yano 98 903 2001 10.1073/pnas.98.3.903 Yano, T. & Kagamiyama, H. Directed evolution of ampicillin-resistant activity from a functionally unrelated DNA fragment: a laboratory model of molecular evolution. Proc. Natl Acad. Sci. USA 98, 903-907 (2001). 

  77. Annu. Rev. Biophys. Biomol. Struct. D Mendel 24 435 1995 10.1146/annurev.bb.24.060195.002251 Mendel, D., Cornish, V. W. & Schultz, P. G. Site-directed mutagenesis with an expanded code. Annu. Rev. Biophys. Biomol. Struct. 24, 435-462 (1995). 

  78. Science L Wang 292 498 2001 10.1126/science.1060077 Wang, L., Brock, A., Herberich, B. & Schultz, P. G. Expanding the genetic code of Escherichia coli. Science 292, 498-504 (2001). 

  79. Proc. Natl Acad. Sci. USA D Kiga 99 9715 2002 10.1073/pnas.142220099 Kiga, D. et al. An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system. Proc. Natl Acad. Sci. USA 99, 9715-9720 (2002). 

  80. J. Biol. Chem. CA Hutchison 253 6551 1978 10.1016/S0021-9258(19)46967-6 Hutchison, C. A. et al. Mutagenesis at a specific position in a DNA sequence. J. Biol. Chem. 253, 6551-6560 (1978). 

  81. Nature Biotechnol. CC Chang 17 793 1999 10.1038/11737 Chang, C. C. et al. Evolution of a cytokine using DNA family shuffling. Nature Biotechnol. 17, 793-797 (1999). 

  82. Nature Biotechnol. V Sieber 19 456 2001 10.1038/88129 Sieber, V., Martinez, C. A. & Arnold, F. H. Libraries of hybrid proteins from distantly related sequences. Nature Biotechnol. 19, 456-460 (2001). 

  83. Nucleic Acids Res. S Lutz 29 16e 2001 10.1093/nar/29.4.e16 Lutz, S., Ostermeier, M. & Benkovic, S. J. Rapid generation of incremental truncation libraries for protein engineering using α-phosphothioate nucleotides. Nucleic Acids Res. 29, 16e (2001). 

  84. Proc. Natl Acad. Sci. USA S Lutz 98 11248 2001 10.1073/pnas.201413698 Lutz, S., Ostermeier, M., Moore, G. L., Maranas, C. D. & Benkovic, S. J. Creating multiple-crossover DNA libraries independent of sequence identity. Proc. Natl Acad. Sci. USA 98, 11248-11253 (2001). 

  85. J. Mol. Biol. PE O'Maille 321 677 2002 10.1016/S0022-2836(02)00675-7 O'Maille, P. E., Bakhtina, M. & Tsai, M. -D. Structure-based combinatorial protein engineering (SCOPE). J. Mol. Biol. 321, 677-691 (2002). 

  86. Physiol. Rev. JV Kilmartin 53 836 1973 10.1152/physrev.1973.53.4.836 Kilmartin, J. V. & Rossi-Bernardi, L. Interaction of haemoglobin with hydrogen ions, carbon dioxide and organic phosphates Physiol. Rev. 53, 836-890 (1973). 

  87. Biochemistry JL Whittingham 36 2826 1997 10.1021/bi9625105 Whittingham, J. L., Havelund, S. & Jonassen, I. Crystal structure of a prolonged-acting insulin with albumin-binding properties. Biochemistry 36, 2826-2831 (1997). 

  88. Nature J McCafferty 348 552 1990 10.1038/348552a0 McCafferty, J., Griffiths, A. D., Winter, G. & Chiswell, D. J. Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348, 552-554 (1990). 

관련 콘텐츠

저작권 관리 안내
섹션별 컨텐츠 바로가기

AI-Helper ※ AI-Helper는 오픈소스 모델을 사용합니다.

AI-Helper 아이콘
AI-Helper
안녕하세요, AI-Helper입니다. 좌측 "선택된 텍스트"에서 텍스트를 선택하여 요약, 번역, 용어설명을 실행하세요.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.

선택된 텍스트

맨위로