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Volumn 7, Issue 9, 1998, Pages 1983-1993

A test of the relationship between sequence and structure in proteins: Excision of the heme binding site in apocytochrome b5

Author keywords

Apocytochrome b5; Heme binding site; Holocytochrome b5; Partially folded protein; Protein folding; Protein stability; Structural specificity

Indexed keywords

APOPROTEIN; CYTOCHROME B5; HEME; HEMOPROTEIN; LINK PROTEIN; LIVER ENZYME;

EID: 0031665756     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070914     Document Type: Article
Times cited : (19)

References (75)
  • 1
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study
    • Alexandrescu AT, Abeygunawardana C, Shortle D. 1994. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study. Biochemistry 33:1063-1072.
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 2
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. 1973. Principles that govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch A. 1991. PROSITE: A dictionary of sites and patterns in proteins. Nucleic Acids Res 19:2241-2245.
    • (1991) Nucleic Acids Res , vol.19 , pp. 2241-2245
    • Bairoch, A.1
  • 6
    • 0025759275 scopus 로고
    • The protein-folding problem: The native fold determines packing, but does packing determine the native fold?
    • Behe MJ, Lattman EE, Rose GD. 1991. The protein-folding problem: The native fold determines packing, but does packing determine the native fold? Proc Natl Acad Sci USA 88:4195-4199.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4195-4199
    • Behe, M.J.1    Lattman, E.E.2    Rose, G.D.3
  • 7
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett MJ, Schlunegger MP, Eisenberg D. 1995. 3D domain swapping: A mechanism for oligomer assembly. Protein Sci 4:2455-2468.
    • (1995) Protein Sci , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 8
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By AA, Stephens RL, Lee J-M, Warren CD, Jeanloz RW. 1984. Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame. J Am Chem Soc 106:811-813.
    • (1984) J Am Chem Soc , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.-M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 11
    • 33748476849 scopus 로고
    • Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence
    • Cavanagh J, Rance M. 1992. Suppression of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J Magn Reson 96:670-678.
    • (1992) J Magn Reson , vol.96 , pp. 670-678
    • Cavanagh, J.1    Rance, M.2
  • 12
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat BI, Mayo SL. 1997. De novo protein design: Fully automated sequence selection. Science 278:82-87.
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 13
    • 0028858499 scopus 로고
    • De novo design of the hydrophobic cores of proteins
    • Desjarlais JR, Handel TM. 1995. De novo design of the hydrophobic cores of proteins. Protein Sci 4:2006-2018.
    • (1995) Protein Sci , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 14
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.1
  • 15
    • 0030948005 scopus 로고    scopus 로고
    • Effects of insertions and deletions in a β-bulge region of Escherichia coli dihydrofolate reductase
    • Dion-Schultz A, Howell EE. 1997. Effects of insertions and deletions in a β-bulge region of Escherichia coli dihydrofolate reductase. Protein Eng 10:263-272.
    • (1997) Protein Eng , vol.10 , pp. 263-272
    • Dion-Schultz, A.1    Howell, E.E.2
  • 19
    • 0029070171 scopus 로고
    • Ω loops: Nonregular secondary structures significant in protein function and stability
    • Fetrow JS. 1995. Ω loops: Nonregular secondary structures significant in protein function and stability. FASEB J 9:708-717.
    • (1995) FASEB J , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 20
    • 0031022598 scopus 로고    scopus 로고
    • Analysis of the structure and stability of Ω loop a replacements in yeast iso-1-cytochrome c
    • Fetrow JS, Horner SR, Oehrl W, Schaak DL, Boose TL, Burton RE. 1997. Analysis of the structure and stability of Ω loop A replacements in yeast iso-1-cytochrome c. Protein Sci 6:197-210.
    • (1997) Protein Sci , vol.6 , pp. 197-210
    • Fetrow, J.S.1    Horner, S.R.2    Oehrl, W.3    Schaak, D.L.4    Boose, T.L.5    Burton, R.E.6
  • 21
    • 0030020571 scopus 로고    scopus 로고
    • Are turns required for the folding of ribonuclease T1?
    • Garrett JB, Mullins LS, Raushel FM. 1996. Are turns required for the folding of ribonuclease T1? Protein Sci 5:204-211.
    • (1996) Protein Sci , vol.5 , pp. 204-211
    • Garrett, J.B.1    Mullins, L.S.2    Raushel, F.M.3
  • 22
    • 0027411746 scopus 로고
    • Effect of point mutation in a flexible loop on the stability and enzymatic activity of Escherichia coli dihydrofolate reductase
    • Gekko K, Yamagami K, Kunori Y, Ichihara S, Kodama M, Iwakura M. 1993. Effect of point mutation in a flexible loop on the stability and enzymatic activity of Escherichia coli dihydrofolate reductase. J Biochem (Tokyo) 113:74-80.
    • (1993) J Biochem (Tokyo) , vol.113 , pp. 74-80
    • Gekko, K.1    Yamagami, K.2    Kunori, Y.3    Ichihara, S.4    Kodama, M.5    Iwakura, M.6
  • 24
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
    • Hamada D, Goto Y. 1997. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. J Mol Biol 269:479-487.
    • (1997) J Mol Biol , vol.269 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 25
    • 0029740071 scopus 로고    scopus 로고
    • Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein
    • Hamada D, Segawa S, Goto Y. 1996. Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct Biol 3:868-873.
    • (1996) Nature Struct Biol , vol.3 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 27
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. 1993. Protein structure comparison by alignment of distance matrices. J Mol Biol 233:123-138.
    • (1993) J Mol Biol , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 30
    • 0028304155 scopus 로고
    • Energy minimization method using automata network for sequence and side-chain conformation prediction from given backbone geometry
    • Kono H, Doi J. 1994. Energy minimization method using automata network for sequence and side-chain conformation prediction from given backbone geometry. Proteins Struct Funct Genet 19:244-255.
    • (1994) Proteins Struct Funct Genet , vol.19 , pp. 244-255
    • Kono, H.1    Doi, J.2
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Applied Cryst 24:946-950.
    • (1991) J Applied Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
  • 33
    • 0019327003 scopus 로고
    • A 2D NOE experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A, Ernst RR, Wüthrich K. 1980. A 2D NOE experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem Biophys Res Commun 95:1-6.
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 34
  • 35
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • Lazar GA, Desjarlais JR, Handel TM. 1997. De novo design of the hydrophobic core of ubiquitin. Protein Sci 6:1167-1178.
    • (1997) Protein Sci , vol.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 36
    • 0000982573 scopus 로고
    • 5. The role of a neutral histidine at the N-cap position
    • 5. The role of a neutral histidine at the N-cap position. J Am Chem Soc 113:9663-9665.
    • (1991) J Am Chem Soc , vol.113 , pp. 9663-9665
    • Lecomte, J.T.J.1    Moore, C.D.2
  • 37
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • Lee JC, Timasheff SN. 1981. The stabilization of proteins by sucrose. J Biol Chem 256:7193-7201.
    • (1981) J Biol Chem , vol.256 , pp. 7193-7201
    • Lee, J.C.1    Timasheff, S.N.2
  • 38
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins
    • Mach H, Middaugh CR, Lewis RV. 1992. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal Biochem 200:74-80.
    • (1992) Anal Biochem , vol.200 , pp. 74-80
    • Mach, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 39
    • 0021902977 scopus 로고
    • The structure, function and evolution of cytochromes
    • Mathews FS. 1985. The structure, function and evolution of cytochromes. Prog Biophys Molec Biol 45:1-56.
    • (1985) Prog Biophys Molec Biol , vol.45 , pp. 1-56
    • Mathews, F.S.1
  • 41
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews CR. 1993. Pathways of protein folding. Annu Rev Biochem 62:653-683.
    • (1993) Annu Rev Biochem , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 42
    • 0029864379 scopus 로고    scopus 로고
    • Collapse and cooperativity in protein folding
    • Miranker AD, Dobson CM. 1996. Collapse and cooperativity in protein folding. Curr Opin Struct Biol 6:31-42.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 31-42
    • Miranker, A.D.1    Dobson, C.M.2
  • 45
    • 0030348048 scopus 로고    scopus 로고
    • Analysis of the effect of local interactions on protein stability
    • Muñoz V, Cronet P, Lopez-Hernandez E, Serrano L. 1996. Analysis of the effect of local interactions on protein stability. Fold Design 1:167-178.
    • (1996) Fold Design , vol.1 , pp. 167-178
    • Muñoz, V.1    Cronet, P.2    Lopez-Hernandez, E.3    Serrano, L.4
  • 46
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace CN. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
    • (1986) Methods Enzymol , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 47
    • 0027338382 scopus 로고
    • 5 unfolding
    • 5 unfolding. Protein Sci 2:1497-1501.
    • (1993) Protein Sci , vol.2 , pp. 1497-1501
    • Pfeil, W.1
  • 48
    • 0025779523 scopus 로고
    • Deletion of the Ω-loop in the active site of staphylococcal nuclease. 1. Effects on catalysis and stability
    • Poole LB, Loveys DA, Hale SP, Gerlt JA, Stanszyk SM, Bolton PH. 1991. Deletion of the Ω-loop in the active site of staphylococcal nuclease. 1. Effects on catalysis and stability. Biochemistry 30:3621-3627.
    • (1991) Biochemistry , vol.30 , pp. 3621-3627
    • Poole, L.B.1    Loveys, D.A.2    Hale, S.P.3    Gerlt, J.A.4    Stanszyk, S.M.5    Bolton, P.H.6
  • 49
    • 0024290488 scopus 로고
    • Helix signals in proteins
    • Presta LG, Rose GD. 1988. Helix signals in proteins. Science 240:1632-1641.
    • (1988) Science , vol.240 , pp. 1632-1641
    • Presta, L.G.1    Rose, G.D.2
  • 50
    • 0031574916 scopus 로고    scopus 로고
    • Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain
    • Prieto J, Wilmans M, Jimenez MA, Rico M, Serrano L. 1997. Non-native local interactions in protein folding and stability: Introducing a helical tendency in the all β-sheet α-spectrin SH3 domain. J Mol Biol 268:760-778.
    • (1997) J Mol Biol , vol.268 , pp. 760-778
    • Prieto, J.1    Wilmans, M.2    Jimenez, M.A.3    Rico, M.4    Serrano, L.5
  • 51
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov PL. 1979. Stability of proteins: Small globular proteins. Adv Prot Chem 33:167-241.
    • (1979) Adv Prot Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 52
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. 1995. Molten globule and protein folding. Adv Prot Chem 47:83-229.
    • (1995) Adv Prot Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 53
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards FM. 1977. Areas, volumes, packing and protein structure. Ann Rev Biophys Bioeng 6:151-171.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 151-171
    • Richards, F.M.1
  • 54
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and the energetics of protein stability
    • Robertson AD, Murphy KP. 1997. Protein structure and the energetics of protein stability. Chem Rev 97:1251-1267.
    • (1997) Chem Rev , vol.97 , pp. 1251-1267
    • Robertson, A.D.1    Murphy, K.P.2
  • 55
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder H, Colon W. 1997. Kinetic role of early intermediates in protein folding. Curr Opin Struct Biol 7:15-28.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 56
    • 0028158628 scopus 로고
    • PHD - An automatic mail server for protein secondary structure prediction
    • Rost B, Sander C, Schneider R. 1994. PHD - An automatic mail server for protein secondary structure prediction. Comp Appl Biosci 10:53-60.
    • (1994) Comp Appl Biosci , vol.10 , pp. 53-60
    • Rost, B.1    Sander, C.2    Schneider, R.3
  • 57
    • 0030803268 scopus 로고    scopus 로고
    • Engineering the independent folding of the subtilisin BPN′ prodomain: Analysis of two-state folding versus protein stability
    • Ruvinov S, Wang L, Ruan B, Almog O, Gilliland GL, Eisenstein E, Bryan PN. 1997. Engineering the independent folding of the subtilisin BPN′ prodomain: Analysis of two-state folding versus protein stability. Biochemistry 36:10414-10421.
    • (1997) Biochemistry , vol.36 , pp. 10414-10421
    • Ruvinov, S.1    Wang, L.2    Ruan, B.3    Almog, O.4    Gilliland, G.L.5    Eisenstein, E.6    Bryan, P.N.7
  • 58
    • 0002983608 scopus 로고    scopus 로고
    • Protein folding from a combinatorial perspective
    • Sauer RT. 1996. Protein folding from a combinatorial perspective. Fold Design 1:R45-R49.
    • (1996) Fold Design , vol.1
    • Sauer, R.T.1
  • 59
    • 0023068366 scopus 로고
    • The thermodynamic stability of proteins
    • Schellman JA. 1987. The thermodynamic stability of proteins. Annu Rev Biophys Biophys Chem 16:115-137.
    • (1987) Annu Rev Biophys Biophys Chem , vol.16 , pp. 115-137
    • Schellman, J.A.1
  • 60
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • New York: IRL Press
    • Schmid FX. 1989. Spectral methods of characterizing protein conformation and conformational changes. In: Protein structure a practical approach. New York: IRL Press. pp 251-285.
    • (1989) Protein Structure a Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 61
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle D. 1996. The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J 10:27-34.
    • (1996) FASEB J , vol.10 , pp. 27-34
    • Shortle, D.1
  • 63
    • 0029055313 scopus 로고
    • LINUS: A hierarchic procedure to predict the fold of a protein
    • Srinivasan R, Rose GD. 1995. LINUS: A hierarchic procedure to predict the fold of a protein. Proteins Struct Funct Genet 22:81-99.
    • (1995) Proteins Struct Funct Genet , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 64
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford C. 1968. Protein denaturation. Adv Prot Chem 23:121-282.
    • (1968) Adv Prot Chem , vol.23 , pp. 121-282
    • Tanford, C.1
  • 65
    • 0014718113 scopus 로고
    • Protein denaturation
    • Tanford C. 1970. Protein denaturation. Adv Prot Chem 24:1-95.
    • (1970) Adv Prot Chem , vol.24 , pp. 1-95
    • Tanford, C.1
  • 66
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky VN. 1993. Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32:13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 67
    • 0029786618 scopus 로고    scopus 로고
    • Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands
    • Uversky VN, Kutyshenko VP, Protasova N, Rogov VV, Vassilenko KS, Gudkov AT. 1996. Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands. Protein Sci 5:1844-1851.
    • (1996) Protein Sci , vol.5 , pp. 1844-1851
    • Uversky, V.N.1    Kutyshenko, V.P.2    Protasova, N.3    Rogov, V.V.4    Vassilenko, K.S.5    Gudkov, A.T.6
  • 68
    • 0030663205 scopus 로고    scopus 로고
    • Loop length, intramolecular diffusion and protein folding
    • Viguera AR, Serrano L. 1997. Loop length, intramolecular diffusion and protein folding. Nature Struct Biol 4:939-946.
    • (1997) Nature Struct Biol , vol.4 , pp. 939-946
    • Viguera, A.R.1    Serrano, L.2
  • 69
    • 0030623698 scopus 로고    scopus 로고
    • Favourable native-like helical local interactions can accelerate protein folding
    • Viguera AR, Villegas V, Avilés FX, Serrano L. 1997. Favourable native-like helical local interactions can accelerate protein folding. Fold Design 2:23-33.
    • (1997) Fold Design , vol.2 , pp. 23-33
    • Viguera, A.R.1    Villegas, V.2    Avilés, F.X.3    Serrano, L.4
  • 70
    • 0030334742 scopus 로고
    • Stabilisation of proteins by rational design of α-helix stability using helix/coil transition theory
    • Villegas V, Viguera AR, Avilés FX, Serrano L. 1995. Stabilisation of proteins by rational design of α-helix stability using helix/coil transition theory. Fold Design 1:29-34.
    • (1995) Fold Design , vol.1 , pp. 29-34
    • Villegas, V.1    Viguera, A.R.2    Avilés, F.X.3    Serrano, L.4
  • 71
    • 0027645554 scopus 로고
    • Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases
    • Vriend G, Eijsink V. 1993. Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases. J Comp-Aided Molec Design 7:367-396.
    • (1993) J Comp-Aided Molec Design , vol.7 , pp. 367-396
    • Vriend, G.1    Eijsink, V.2
  • 72
    • 0027542118 scopus 로고
    • Quality control of protein models: Directional atomic contact analysis
    • Vriend G, Sander C. 1993. Quality control of protein models: Directional atomic contact analysis. J Appl Cryst 26:47-60.
    • (1993) J Appl Cryst , vol.26 , pp. 47-60
    • Vriend, G.1    Sander, C.2
  • 73
    • 0029806946 scopus 로고    scopus 로고
    • Perturbations of the denatured state ensemble: Modeling their effects on protein stability and kinetics
    • Wrabl JO, Shortle D. 1996. Perturbations of the denatured state ensemble: Modeling their effects on protein stability and kinetics. Protein Sci 5:2343-2352.
    • (1996) Protein Sci , vol.5 , pp. 2343-2352
    • Wrabl, J.O.1    Shortle, D.2
  • 74
    • 0031565731 scopus 로고    scopus 로고
    • Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease D131D, using NMR methods with improved resolution
    • Zhang O, Kay LE, Shortle D, Forman-Kay JD. 1997. Comprehensive NOE characterization of a partially folded large fragment of staphylococcal nuclease D131D, using NMR methods with improved resolution. J Mol Biol 272:9-20.
    • (1997) J Mol Biol , vol.272 , pp. 9-20
    • Zhang, O.1    Kay, L.E.2    Shortle, D.3    Forman-Kay, J.D.4
  • 75
    • 0029585945 scopus 로고
    • Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive
    • Zhang XJ, Baase WA, Shoichet BK, Wilson KP, Matthews BW. 1995. Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive. Protein Eng 8:1017-1022.
    • (1995) Protein Eng , vol.8 , pp. 1017-1022
    • Zhang, X.J.1    Baase, W.A.2    Shoichet, B.K.3    Wilson, K.P.4    Matthews, B.W.5


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