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Volumn 35, Issue , 2006, Pages 49-65

Computer-based design of novel protein structures

Author keywords

Computational protein design; Flexible backbone design; Molecular modeling; Negative design; Protein stability

Indexed keywords

AMINO ACID; MEMBRANE PROTEIN;

EID: 33745033790     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.35.040405.102046     Document Type: Review
Times cited : (114)

References (83)
  • 1
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • Baldwin EP, Hajiseyedjavadi O, Baase WA, Matthews BW. 1993. The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. Science 262:1715-18
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase, W.A.3    Matthews, B.W.4
  • 3
    • 24944493938 scopus 로고    scopus 로고
    • Toward high-resolution de novo structure prediction for small proteins
    • Bradley P, Misura KM, Baker D. 2005. Toward high-resolution de novo structure prediction for small proteins. Science 309:1868-71
    • (2005) Science , vol.309 , pp. 1868-1871
    • Bradley, P.1    Misura, K.M.2    Baker, D.3
  • 7
    • 0000747247 scopus 로고
    • The Fourier transform of a coiled-coil
    • Crick FHC. 1953. The Fourier transform of a coiled-coil. Acta Crystallogr. 6:685-89
    • (1953) Acta Crystallogr. , vol.6 , pp. 685-689
    • Crick, F.H.C.1
  • 8
    • 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
  • 9
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat BI, Mayo SL. 1997. Probing the role of packing specificity in protein design. Proc. Natl. Acad. Sci. USA 94:10172-77
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 11
    • 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. 4:2006-18
    • (1995) Protein Sci. , vol.4 , pp. 2006-2018
    • Desjarlais, J.R.1    Handel, T.M.2
  • 12
    • 0033516509 scopus 로고    scopus 로고
    • Side-chain and backbone flexibility in protein core design
    • Desjarlais JR, Handel TM. 1999. Side-chain and backbone flexibility in protein core design. J. Mol. Biol. 290:305-18
    • (1999) J. Mol. Biol. , vol.290 , pp. 305-318
    • Desjarlais, J.R.1    Handel, T.M.2
  • 13
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • Desmet J, Maeyer MD, Hazes B, Lasters I. 1992. The dead-end elimination theorem and its use in protein side-chain positioning. Nature 356:539-41
    • (1992) Nature , vol.356 , pp. 539-541
    • Desmet, J.1    Maeyer, M.D.2    Hazes, B.3    Lasters, I.4
  • 14
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • Dunbrack RL Jr, Cohen FE. 1997. Bayesian statistical analysis of protein side-chain rotamer preferences. Protein Sci. 6:1661-81
    • (1997) Protein Sci. , vol.6 , pp. 1661-1681
    • Dunbrack Jr., R.L.1    Cohen, F.E.2
  • 15
    • 3042655537 scopus 로고    scopus 로고
    • Computational design of a biologically active enzyme
    • Dwyer MA, Looger LL, Hellinga HW. 2004. Computational design of a biologically active enzyme. Science 304:1967-71
    • (2004) Science , vol.304 , pp. 1967-1971
    • Dwyer, M.A.1    Looger, L.L.2    Hellinga, H.W.3
  • 18
    • 0036291145 scopus 로고    scopus 로고
    • Predicting changes in the stability of proteins and protein complexes: A study of more than 1000 mutations
    • Guerois R, Nielsen JE, Serrano L. 2002. Predicting changes in the stability of proteins and protein complexes: a study of more than 1000 mutations. J. Mol. Biol. 320:309-87
    • (2002) J. Mol. Biol. , vol.320 , pp. 309-387
    • Guerois, R.1    Nielsen, J.E.2    Serrano, L.3
  • 20
    • 0029091449 scopus 로고
    • Repacking protein cores with backbone freedom: Structure prediction for coiled coils
    • Harbury PB, Tidor B, Kim PS. 1995. Repacking protein cores with backbone freedom: structure prediction for coiled coils. Proc. Natl. Acad. Sci. USA 92:8408-12
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8408-8412
    • Harbury, P.B.1    Tidor, B.2    Kim, P.S.3
  • 21
    • 0033613164 scopus 로고    scopus 로고
    • Tanford-Kirkwood electrostatics for protein modeling
    • Havranek JJ, Harbury PB. 1999. Tanford-Kirkwood electrostatics for protein modeling. Proc. Natl. Acad. Sci. USA 96:11145-50
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11145-11150
    • Havranek, J.J.1    Harbury, P.B.2
  • 22
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • Havranek JJ, Harbury PB. 2003. Automated design of specificity in molecular recognition. Nat. Struct. Biol. 10:45-52
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 23
    • 23844455986 scopus 로고    scopus 로고
    • Adaptation of a fast Fourier transform-based docking algorithm for protein design
    • Huang PS, Love JJ, Mayo SL. 2005. Adaptation of a fast Fourier transform-based docking algorithm for protein design. J. Comput. Chem. 26:1222-32
    • (2005) J. Comput. Chem. , vol.26 , pp. 1222-1232
    • Huang, P.S.1    Love, J.J.2    Mayo, S.L.3
  • 25
    • 0038242197 scopus 로고    scopus 로고
    • De novo design of foldable proteins with smooth folding funnel: Automated negative design and experimental verification
    • Jin W, Kambara O, Sasakawa H, Tamura A, Takada S. 2003. De novo design of foldable proteins with smooth folding funnel: automated negative design and experimental verification. Structure 11:581-90
    • (2003) Structure , vol.11 , pp. 581-590
    • Jin, W.1    Kambara, O.2    Sasakawa, H.3    Tamura, A.4    Takada, S.5
  • 26
    • 0035909890 scopus 로고    scopus 로고
    • Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils
    • Keating AE, Malashkevich VN, Tidor B, Kim PS. 2001. Side-chain repacking calculations for predicting structures and stabilities of heterodimeric coiled coils. Proc. Natl. Acad. Sci. USA 98:14825-30
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14825-14830
    • Keating, A.E.1    Malashkevich, V.N.2    Tidor, B.3    Kim, P.S.4
  • 27
    • 0028343413 scopus 로고
    • Application of a self-consistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy
    • Koehl P, Delarue M. 1994. Application of a self-consistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy. J. Mol. Biol. 239:249-75
    • (1994) J. Mol. Biol. , vol.239 , pp. 249-275
    • Koehl, P.1    Delarue, M.2
  • 28
    • 0033550264 scopus 로고    scopus 로고
    • De novo protein design. II. Plasticity in sequence space
    • Koehl P, Levitt M. 1999. De novo protein design. II. Plasticity in sequence space. J. Mol. Biol. 293:1183-93
    • (1999) J. Mol. Biol. , vol.293 , pp. 1183-1193
    • Koehl, P.1    Levitt, M.2
  • 29
    • 0035936702 scopus 로고    scopus 로고
    • Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure
    • Kono H, Saven JG. 2001. Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure. J. Mol. Biol. 306:607-28
    • (2001) J. Mol. Biol. , vol.306 , pp. 607-628
    • Kono, H.1    Saven, J.G.2
  • 30
    • 1042298843 scopus 로고    scopus 로고
    • Computational design of protein-protein interactions
    • Kortemme T, Baker D. 2004. Computational design of protein-protein interactions. Curr. Opin. Chem. Biol. 8:91-97
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 91-97
    • Kortemme, T.1    Baker, D.2
  • 31
    • 0037470581 scopus 로고    scopus 로고
    • An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes
    • Kortemme T, Morozov AV, Baker D. 2003. An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes. J. Mol. Biol. 326:1239-59
    • (2003) J. Mol. Biol. , vol.326 , pp. 1239-1259
    • Kortemme, T.1    Morozov, A.V.2    Baker, D.3
  • 33
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • Kuhlman B, Baker D. 2000. Native protein sequences are close to optimal for their structures. Proc. Natl. Acad. Sci. USA 97:10383-88
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 34
    • 1342324030 scopus 로고    scopus 로고
    • Exploring folding free energy landscapes using computational protein design
    • Kuhlman B, Baker D. 2004. Exploring folding free energy landscapes using computational protein design. Curr. Opin. Struct. Biol. 14:89-95
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 89-95
    • Kuhlman, B.1    Baker, D.2
  • 36
    • 0036300662 scopus 로고    scopus 로고
    • Accurate computer-based design of a new backbone conformation in the second turn of protein L
    • Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D. 2002. Accurate computer-based design of a new backbone conformation in the second turn of protein L. J. Mol. Biol. 315:471-77
    • (2002) J. Mol. Biol. , vol.315 , pp. 471-477
    • Kuhlman, B.1    O'Neill, J.W.2    Kim, D.E.3    Zhang, K.Y.4    Baker, D.5
  • 38
    • 0036892389 scopus 로고    scopus 로고
    • Thoroughly sampling sequence space: Large-scale protein design of structural ensembles
    • Larson SM, England JL, Desjarlais JR, Pande VS. 2002. Thoroughly sampling sequence space: large-scale protein design of structural ensembles. Protein Sci. 11:2804-13
    • (2002) Protein Sci. , vol.11 , pp. 2804-2813
    • Larson, S.M.1    England, J.L.2    Desjarlais, J.R.3    Pande, V.S.4
  • 39
    • 0037547120 scopus 로고    scopus 로고
    • Increased detection of structural templates using alignments of designed sequences
    • Larson SM, Garg A, Desjarlais JR, Pande VS. 2003. Increased detection of structural templates using alignments of designed sequences. Proteins 51:390-96
    • (2003) Proteins , vol.51 , pp. 390-396
    • Larson, S.M.1    Garg, A.2    Desjarlais, J.R.3    Pande, V.S.4
  • 41
    • 0025372503 scopus 로고
    • The design of idealized alpha/beta-barrels: Analysis of beta-sheet closure requirements
    • Lasters I, Wodak SJ, Pio F. 1990. The design of idealized alpha/beta-barrels: analysis of beta-sheet closure requirements. Proteins 7:249-56
    • (1990) Proteins , vol.7 , pp. 249-256
    • Lasters, I.1    Wodak, S.J.2    Pio, F.3
  • 42
    • 0034031680 scopus 로고    scopus 로고
    • Effective energy functions for protein structure prediction
    • Lazaridis T, Karplus M. 2000. Effective energy functions for protein structure prediction. Curr. Opin. Struct. Biol. 10:139-45
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 139-145
    • Lazaridis, T.1    Karplus, M.2
  • 43
    • 0036149564 scopus 로고    scopus 로고
    • Side-chain modeling with an optimized scoring function
    • Liang S, Grishin NV. 2002. Side-chain modeling with an optimized scoring function. Protein Sci. 11:322-31
    • (2002) Protein Sci. , vol.11 , pp. 322-331
    • Liang, S.1    Grishin, N.V.2
  • 44
    • 0347089142 scopus 로고    scopus 로고
    • Effective scoring function for protein sequence design
    • Liang S, Grishin NV. 2004. Effective scoring function for protein sequence design. Proteins 54:271-81
    • (2004) Proteins , vol.54 , pp. 271-281
    • Liang, S.1    Grishin, N.V.2
  • 45
    • 0028147533 scopus 로고
    • The crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lim WA, Hodel A, Sauer RT, Richards FM. 1994. The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl. Acad. Sci. USA 91:423-27
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, F.M.4
  • 46
    • 0034612192 scopus 로고    scopus 로고
    • Inaugural article: Retrostructural analysis of metalloproteins: Application to the design of a minimal model for diiron proteins
    • Lombardi A, Summa CM, Geremia S, Randaccio L, Pavone V, DeGrado WF. 2000. Inaugural article: retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins. Proc. Natl. Acad. Sci. USA 97:6298-305
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6298-6305
    • Lombardi, A.1    Summa, C.M.2    Geremia, S.3    Randaccio, L.4    Pavone, V.5    Degrado, W.F.6
  • 47
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • Looger LL, Dwyer MA, Smith JJ, Hellinga HW. 2003. Computational design of receptor and sensor proteins with novel functions. Nature 423:185-90
    • (2003) Nature , vol.423 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith, J.J.3    Hellinga, H.W.4
  • 48
    • 0035896029 scopus 로고    scopus 로고
    • Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: Implications for protein design and structural genomics
    • Looger LL, Hellinga HW. 2001. Generalized dead-end elimination algorithms make large-scale protein side-chain structure prediction tractable: implications for protein design and structural genomics. J. Mol. Biol. 307:429-45
    • (2001) J. Mol. Biol. , vol.307 , pp. 429-445
    • Looger, L.L.1    Hellinga, H.W.2
  • 50
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malakauskas SM, Mayo SL. 1998. Design, structure and stability of a hyperthermophilic protein variant. Nat. Struct. Biol. 5:470-75
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 52
    • 2342593131 scopus 로고    scopus 로고
    • Close agreement between the orientation dependence of hydrogen bonds observed in protein structures and quantum mechanical calculations
    • Morozov AV, Kortemme T, Tsemekhman K, Baker D. 2004. Close agreement between the orientation dependence of hydrogen bonds observed in protein structures and quantum mechanical calculations. Proc. Natl. Acad. Sci. USA 101:6946-51
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6946-6951
    • Morozov, A.V.1    Kortemme, T.2    Tsemekhman, K.3    Baker, D.4
  • 53
    • 0028348081 scopus 로고
    • Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis
    • Murzin AG, Lesk AM, Chothia C. 1994. Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis. J. Mol. Biol. 236:1369-81
    • (1994) J. Mol. Biol. , vol.236 , pp. 1369-1381
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 54
    • 0028330220 scopus 로고
    • Principles determining the structure of beta-sheet barrels in proteins. II. The observed structures
    • Murzin AG, Lesk AM, Chothia C. 1994. Principles determining the structure of beta-sheet barrels in proteins. II. The observed structures. J. Mol. Biol. 236:1382-400
    • (1994) J. Mol. Biol. , vol.236 , pp. 1382-1400
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 55
    • 0037261324 scopus 로고    scopus 로고
    • De novo backbone and sequence design of an idealized alpha/beta-barrel protein: Evidence of stable tertiary structure
    • Offredi F, Dubail F, Kischel P, Sarinski K, Stern AS, et al. 2003. De novo backbone and sequence design of an idealized alpha/beta-barrel protein: evidence of stable tertiary structure. J. Mol. Biol. 325:163-74
    • (2003) J. Mol. Biol. , vol.325 , pp. 163-174
    • Offredi, F.1    Dubail, F.2    Kischel, P.3    Sarinski, K.4    Stern, A.S.5
  • 57
    • 4143120071 scopus 로고    scopus 로고
    • Structural test of the parameterized-backbone method for protein design
    • Plecs JJ, Harbury PB, Kim PS, Alber T. 2004. Structural test of the parameterized-backbone method for protein design. J. Mol. Biol. 342:289-97
    • (2004) J. Mol. Biol. , vol.342 , pp. 289-297
    • Plecs, J.J.1    Harbury, P.B.2    Kim, P.S.3    Alber, T.4
  • 58
    • 0035782661 scopus 로고    scopus 로고
    • Review, protein design-where we were, where we are, where we're going
    • Pokala N, Handel TM. 2001. Review, protein design-where we were, where we are, where we're going. J. Struct. Biol. 134:269-81
    • (2001) J. Struct. Biol. , vol.134 , pp. 269-281
    • Pokala, N.1    Handel, T.M.2
  • 59
    • 1842454839 scopus 로고    scopus 로고
    • Energy functions for protein design. I. Efficient and accurate continuum electrostatics and solvation
    • Pokala N, Handel TM. 2004. Energy functions for protein design. I. Efficient and accurate continuum electrostatics and solvation. Protein Sci. 13:925-36
    • (2004) Protein Sci. , vol.13 , pp. 925-936
    • Pokala, N.1    Handel, T.M.2
  • 60
    • 14144256681 scopus 로고    scopus 로고
    • Energy functions for protein design: Adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity
    • Pokala N, Handel TM. 2005. Energy functions for protein design: adjustment with protein-protein complex affinities, models for the unfolded state, and negative design of solubility and specificity. J. Mol. Biol. 347:203-27
    • (2005) J. Mol. Biol. , vol.347 , pp. 203-227
    • Pokala, N.1    Handel, T.M.2
  • 61
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder JW, Richards FM. 1987. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193:775-91
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 65
    • 0035109198 scopus 로고    scopus 로고
    • Designed protein G core variants fold to native-like structures: Sequence selection by ORBIT tolerates variation in backbone specification
    • Ross SA, Sarisky CA, Su A, Mayo SL. 2001. Designed protein G core variants fold to native-like structures: Sequence selection by ORBIT tolerates variation in backbone specification. Protein Sci. 10:450-54
    • (2001) Protein Sci. , vol.10 , pp. 450-454
    • Ross, S.A.1    Sarisky, C.A.2    Su, A.3    Mayo, S.L.4
  • 66
    • 12544260150 scopus 로고    scopus 로고
    • Recapitulation of protein family divergence using flexible backbone protein design
    • Saunders CT, Baker D. 2005. Recapitulation of protein family divergence using flexible backbone protein design. J. Mol. Biol. 346:631-44
    • (2005) J. Mol. Biol. , vol.346 , pp. 631-644
    • Saunders, C.T.1    Baker, D.2
  • 67
    • 0344392711 scopus 로고    scopus 로고
    • Exploring the origins of binding specificity through the computational redesign of calmodulin
    • Shifman JM, Mayo SL. 2003. Exploring the origins of binding specificity through the computational redesign of calmodulin. Proc. Natl. Acad. Sci. USA 100:13274-79
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13274-13279
    • Shifman, J.M.1    Mayo, S.L.2
  • 69
    • 0021844602 scopus 로고
    • Beta-hairpin families in globular proteins
    • Sibanda BL, Thornton JM. 1985. Beta-hairpin families in globular proteins. Nature 316:170-74
    • (1985) Nature , vol.316 , pp. 170-174
    • Sibanda, B.L.1    Thornton, J.M.2
  • 70
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons KT, Kooperberg C, Huang E, Baker D. 1997. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268:209-25
    • (1997) J. Mol. Biol. , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 71
    • 0032929780 scopus 로고    scopus 로고
    • Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins
    • Simons KT, Ruczinski I, Kooperberg C, Fox BA, Bystroff C, Baker D. 1999. Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins. Proteins 34:82-95
    • (1999) Proteins , vol.34 , pp. 82-95
    • Simons, K.T.1    Ruczinski, I.2    Kooperberg, C.3    Fox, B.A.4    Bystroff, C.5    Baker, D.6
  • 73
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by docking methods
    • Smith GR, Sternberg MJ. 2002. Prediction of protein-protein interactions by docking methods. Curr. Opin. Struct. Biol. 12:28-35
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 28-35
    • Smith, G.R.1    Sternberg, M.J.2
  • 74
    • 0031844416 scopus 로고    scopus 로고
    • Pairwise calculation of protein solvent-accessible surface areas
    • Street AG, Mayo SL. 1998. Pairwise calculation of protein solvent-accessible surface areas. Fold. Des. 3:253-58
    • (1998) Fold. Des. , vol.3 , pp. 253-258
    • Street, A.G.1    Mayo, S.L.2
  • 75
    • 0030762021 scopus 로고    scopus 로고
    • Coupling backbone flexibility and amino acid sequence selection in protein design
    • Su A, Mayo SL. 1997. Coupling backbone flexibility and amino acid sequence selection in protein design. Protein Sci. 6:1701-7
    • (1997) Protein Sci. , vol.6 , pp. 1701-1707
    • Su, A.1    Mayo, S.L.2
  • 77
    • 0036385840 scopus 로고    scopus 로고
    • Computational de novo design, and characterization of an A(2)B(2) diiron protein
    • Summa CM, Rosenblatt MM, Hong JK, Lear JD, DeGrado WF. 2002. Computational de novo design, and characterization of an A(2)B(2) diiron protein. J. Mol. Biol. 321:923-38
    • (2002) J. Mol. Biol. , vol.321 , pp. 923-938
    • Summa, C.M.1    Rosenblatt, M.M.2    Hong, J.K.3    Lear, J.D.4    Degrado, W.F.5
  • 78
    • 2642514014 scopus 로고    scopus 로고
    • Designing proteins from the inside out
    • 77a. Ventura S, Serrano L. 2004. Designing proteins from the inside out. Proteins 56:1-10
    • (2004) Proteins , vol.56 , pp. 1-10
    • Ventura, S.1    Serrano, L.2
  • 79
    • 0034625322 scopus 로고    scopus 로고
    • Trading accuracy for speed: A quantitative comparison of search algorithms in protein sequence design
    • Voigt CA, Gordon DB, Mayo SL. 2000. Trading accuracy for speed: a quantitative comparison of search algorithms in protein sequence design. J. Mol. Biol. 299:789-803
    • (2000) J. Mol. Biol. , vol.299 , pp. 789-803
    • Voigt, C.A.1    Gordon, D.B.2    Mayo, S.L.3
  • 80
    • 0019316535 scopus 로고
    • Structural and functional diversity in 4-alpha-helical proteins
    • Weber PC, Salemme FR. 1980. Structural and functional diversity in 4-alpha-helical proteins. Nature 287:82-84
    • (1980) Nature , vol.287 , pp. 82-84
    • Weber, P.C.1    Salemme, F.R.2
  • 81
    • 0034682869 scopus 로고    scopus 로고
    • Automatic protein design with all atom force-fields by exact and heuristic optimization
    • Wernisch L, Hery S, Wodak SJ. 2000. Automatic protein design with all atom force-fields by exact and heuristic optimization. J. Mol. Biol. 301:713-36
    • (2000) J. Mol. Biol. , vol.301 , pp. 713-736
    • Wernisch, L.1    Hery, S.2    Wodak, S.J.3
  • 82
    • 0037963208 scopus 로고    scopus 로고
    • An empirical model for electrostatic interactions in proteins incorporating multiple geometry-dependent dielectric constants
    • Wisz MS, Hellinga HW. 2003. An empirical model for electrostatic interactions in proteins incorporating multiple geometry-dependent dielectric constants. Proteins 51:360-77
    • (2003) Proteins , vol.51 , pp. 360-377
    • Wisz, M.S.1    Hellinga, H.W.2
  • 83
    • 0035914473 scopus 로고    scopus 로고
    • Virtual interaction profiles of proteins
    • Wollacott AM, Desjarlais JR. 2001. Virtual interaction profiles of proteins. J. Mol. Biol. 313:317-42
    • (2001) J. Mol. Biol. , vol.313 , pp. 317-342
    • Wollacott, A.M.1    Desjarlais, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.