메뉴 건너뛰기




Volumn 14, Issue 4, 2004, Pages 487-494

Advances in computational protein design

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN;

EID: 4143150944     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.06.002     Document Type: Review
Times cited : (79)

References (55)
  • 1
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • B.I. Dahiyat, and S.L. Mayo De novo protein design: fully automated sequence selection Science 278 1997 82 87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat1    Mayo, S.L.B.I.2
  • 2
    • 2642670311 scopus 로고    scopus 로고
    • Design of a 20-amino acid, three-stranded beta-sheet protein
    • T. Kortemme, M. Ramirez-Alvarado, and L. Serrano Design of a 20-amino acid, three-stranded beta-sheet protein Science 281 1998 253 256
    • (1998) Science , vol.281 , pp. 253-256
    • Kortemme, T.1    Ramirez-Alvarado2    Serrano, L.M.3
  • 3
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • P.B. Harbury, J.J. Plecs, B. Tidor, T. Alber, and P.S. Kim High-resolution protein design with backbone freedom Science 282 1998 1462 1467
    • (1998) Science , vol.282 , pp. 1462-1467
    • Harbury, P.B.1    Plecs, J.J.2    Tidor, B.3    Alber4    Kim, P.S.T.5
  • 4
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain retainer preferences
    • R. Dunbrack, and F.E. Cohen Bayesian statistical analysis of protein side-chain retainer preferences Protein Sci 6 1997 1661 1681
    • (1997) Protein Sci , vol.6 , pp. 1661-1681
    • Dunbrack1    Cohen, F.E.R.2
  • 5
    • 0034625322 scopus 로고    scopus 로고
    • Trading accuracy for speed: A quantitative comparison of search algorithms in protein sequence design
    • C.A. Voigt, D.B. Gordon, and S.L. Mayo Trading accuracy for speed: a quantitative comparison of search algorithms in protein sequence design J Mol Biol 299 2000 789 803
    • (2000) J Mol Biol , vol.299 , pp. 789-803
    • Voigt, C.A.1    Gordon2    Mayo, S.L.D.B.3
  • 6
    • 0035936702 scopus 로고    scopus 로고
    • Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure
    • H. Kono, and J.G. Saven Statistical theory for protein combinatorial libraries. Packing interactions, backbone flexibility, and the sequence variability of a main-chain structure J Mol Biol 306 2001 607 628
    • (2001) J Mol Biol , vol.306 , pp. 607-628
    • Kono1    Saven, J.G.H.2
  • 8
    • 0041530316 scopus 로고    scopus 로고
    • NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics
    • B. Gillespie, D.M. Vu, P.S. Shah, S.A. Marshall, R.B. Dyer, S.L. Mayo, and K.W. Plaxco NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics J Mol Biol 330 2003 813 819 De novo computationally designed proteins are found to fold on timescales of 10-50 μs, suggesting that fast folding is consistent with high stability and close to optimal interatomic interactions in the folded state.
    • (2003) J Mol Biol , vol.330 , pp. 813-819
    • Gillespie, B.1    Vu, D.M.2    Shah, P.S.3    Marshall, S.A.4    Dyer, R.B.5    Mayo6    Plaxco, K.W.S.L.7
  • 9
    • 0346734133 scopus 로고    scopus 로고
    • Ultrafast folding of alpha3D: A de novo designed three-helix bundle protein
    • Y. Zhu, D.O. Alonso, K. Maki, C.Y. Huang, S.J. Lahr, V. Daggett, H. Roder, W.F. DeGrado, and F. Gai Ultrafast folding of alpha3D: a de novo designed three-helix bundle protein Proc Natl Acad Sci USA 100 2003 15486 15491 The authors studied the folding of a de novo designed three-helix-bundle protein using IR spectroscopy, temperature jump spectroscopy and molecular dynamics simulation. The protein is found to fold on a microsecond timescale and has a highly heterogeneous set of folding trajectories.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15486-15491
    • Zhu, Y.1    Alonso, D.O.2    Maki, K.3    Huang, C.Y.4    Lahr, S.J.5    Daggett, V.6    Roder, H.7    Degrado8    Gai, F.W.F.9
  • 10
    • 4143101125 scopus 로고    scopus 로고
    • Guiding the search for a protein's maximum rate of folding
    • in press.
    • Zhu Y, Fu X, Wang T, Tamura A, Takada S, Saven JG, Gai F: Guiding the search for a protein's maximum rate of folding. Chem Phys 2004, in press. Statistical computational design was used to identify "frustrated" sites in a 47-residue three-helix-bundle protein and to identify mutations that modulate hydrophobic content consistent with the folded structure. Several mutants were made and experimentally characterized. Correlation of the folding rate with tailored hydrophobic mutations is observed. One double mutant is among the fastest folding proteins known, with a folding time of 1 μs.
    • (2004) Chem Phys
    • Zhu, Y.1    Fu, X.2    Wang, T.3    Tamura, A.4    Takada, S.5    Saven, J.G.6    Gai, F.7
  • 11
    • 0030628825 scopus 로고    scopus 로고
    • Theory of protein folding: The energy landscape perspective
    • J.N. Onuchic, Z. Luthey-Schulten, and P.G. Wolynes Theory of protein folding: the energy landscape perspective Annu Rev Phys Chem 48 1997 545 600
    • (1997) Annu Rev Phys Chem , vol.48 , pp. 545-600
    • Onuchic, J.N.1    Luthey-Schulten2    Wolynes, P.G.Z.3
  • 12
    • 0038242197 scopus 로고    scopus 로고
    • De novo design of foldable proteins with smooth folding funnel: Automated negative design and experimental verification
    • W. Jin, O. Kambara, H. Sasakawa, A. Tamura, and S. Takada De novo design of foldable proteins with smooth folding funnel: automated negative design and experimental verification Structure 11 2003 581 590 The authors designed a three-helix-bundle topology and selected several of the designed sequences for synthesis. The design principle involves selecting for the global shape of the protein folding funnel, whereby sequences are identified that have the target structure as the lowest energy state among all the structures sampled by many folding simulations. The authors use a coarse-grained protein model with simplified sidechain representations. NMR and CD spectroscopic data indicate that one designed sequence has a well-defined three-dimensional structure and helical content consistent with the target. This work provides an elegant synthesis of energy landscape ideas and protein design methods.
    • (2003) Structure , vol.11 , pp. 581-590
    • Jin, W.1    Kambara, O.2    Sasakawa, H.3    Tamura4    Takada, S.A.5
  • 13
    • 0036385840 scopus 로고    scopus 로고
    • Computational de novo design, and characterization of an A(2)B(2) diiron protein
    • C.M. Summa, M.M. Rosenblatt, J.K. Hong, J.D. Lear, and W.F. DeGrado Computational de novo design, and characterization of an A(2)B(2) diiron protein J Mol Biol 321 2002 923 938 A simple parameterization of complementary electrostatic interactions in a four-helix bundle is used to design a four-helix heterotetramer. This represents one of the first computational efforts with explicit negative design and experimental verification.
    • (2002) J Mol Biol , vol.321 , pp. 923-938
    • Summa, C.M.1    Rosenblatt, M.M.2    Hong, J.K.3    Lear4    Degrado, W.F.J.D.5
  • 14
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • J.J. Havranek, and P.B. Harbury Automated design of specificity in molecular recognition Nat Struct Biol 10 2003 45 52
    • (2003) Nat Struct Biol , vol.10 , pp. 45-52
    • Havranek1    Harbury, P.B.J.J.2
  • 15
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • B. Kuhlman, G. Dantas, G.C. Ireton, G. Varani, B.L. Stoddard, and D. Baker Design of a novel globular protein fold with atomic-level accuracy Science 302 2003 1364 1368 A novel 93-residue α/β protein structure is identified and computationally designed. The crystallographic structure of one sequence is within 1.7 Å of the structure obtained from the calculation.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard5    Baker, D.B.L.6
  • 16
    • 0036407643 scopus 로고    scopus 로고
    • Modulating calmodulin binding specificity through computational protein design
    • J.M. Shifman, and S.L. Mayo Modulating calmodulin binding specificity through computational protein design J Mol Biol 323 2002 417 423
    • (2002) J Mol Biol , vol.323 , pp. 417-423
    • Shifman1    Mayo, S.L.J.M.2
  • 18
    • 0028858499 scopus 로고
    • De-novo design of the hydrophobic cores of proteins
    • J.R. Desjarlais, and T.M. Handel De-novo design of the hydrophobic cores of proteins Protein Sci 4 1995 2006 2018
    • (1995) Protein Sci , vol.4 , pp. 2006-2018
    • Desjarlais1    Handel, T.M.J.R.2
  • 19
    • 0347089142 scopus 로고    scopus 로고
    • Effective scoring function for protein sequence design
    • S. Liang, and N.V. Grishin Effective scoring function for protein sequence design Proteins 54 2004 271 281
    • (2004) Proteins , vol.54 , pp. 271-281
    • Liang1    Grishin, N.V.S.2
  • 20
    • 1342310514 scopus 로고    scopus 로고
    • Improved side-chain prediction accuracy using an ab initio potential energy function and a very large rotamer library
    • R.W. Peterson, P.L. Dutton, and A.J. Wand Improved side-chain prediction accuracy using an ab initio potential energy function and a very large rotamer library Protein Sci 13 2004 735 751
    • (2004) Protein Sci , vol.13 , pp. 735-751
    • Peterson, R.W.1    Dutton2    Wand, A.J.P.L.3
  • 21
    • 0032929780 scopus 로고    scopus 로고
    • Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins
    • K.T. Simons, I. Ruczinski, C. Kooperberg, B.A. Fox, C. Bystroff, and D. Baker Improved recognition of native-like protein structures using a combination of sequence-dependent and sequence-independent features of proteins Proteins 34 1999 82 95
    • (1999) Proteins , vol.34 , pp. 82-95
    • Simons, K.T.1    Ruczinski, I.2    Kooperberg, C.3    Fox, B.A.4    Bystroff5    Baker, D.C.6
  • 22
    • 0021192240 scopus 로고
    • Hydrogen bonding in globular proteins
    • E.N. Baker, and R.E. Hubbard Hydrogen bonding in globular proteins Prog Biophys Mol Biol 44 1984 97 179
    • (1984) Prog Biophys Mol Biol , vol.44 , pp. 97-179
    • Baker1    Hubbard, R.E.E.N.2
  • 23
    • 0037470581 scopus 로고    scopus 로고
    • An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes
    • T. Kortemme, A.V. Morozov, and D. Baker An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes J Mol Biol 326 2003 1239 1259
    • (2003) J Mol Biol , vol.326 , pp. 1239-1259
    • Kortemme, T.1    Morozov2    Baker, D.A.V.3
  • 24
    • 0037954108 scopus 로고    scopus 로고
    • Prudent modeling of core polar residues in computational protein design
    • D.N. Bolon, J.S. Marcus, S.A. Ross, and S.L. Mayo Prudent modeling of core polar residues in computational protein design J Mol Biol 329 2003 611 622
    • (2003) J Mol Biol , vol.329 , pp. 611-622
    • Bolon, D.N.1    Marcus, J.S.2    Ross3    Mayo, S.L.S.A.4
  • 25
    • 0038752617 scopus 로고    scopus 로고
    • Computational design of receptor and sensor proteins with novel functions
    • L.L. Looger, M.A. Dwyer, J.J. Smith, and H.W. Hellinga Computational design of receptor and sensor proteins with novel functions Nature 423 2003 185 190
    • (2003) Nature , vol.423 , pp. 185-190
    • Looger, L.L.1    Dwyer, M.A.2    Smith3    Hellinga, H.W.J.J.4
  • 26
    • 0036307678 scopus 로고    scopus 로고
    • Electrostatics significantly affect the stability of designed homeodomain variants
    • S.A. Marshall, C.S. Morgan, and S.L. Mayo Electrostatics significantly affect the stability of designed homeodomain variants J Mol Biol 316 2002 189 199
    • (2002) J Mol Biol , vol.316 , pp. 189-199
    • Marshall, S.A.1    Morgan2    Mayo, S.L.C.S.3
  • 27
    • 0037963208 scopus 로고    scopus 로고
    • An empirical model for electrostatic interactions in proteins incorporating multiple geometry-dependent dielectric constants
    • M.S. Wisz, and H.W. Hellinga An empirical model for electrostatic interactions in proteins incorporating multiple geometry-dependent dielectric constants Proteins 51 2003 360 377
    • (2003) Proteins , vol.51 , pp. 360-377
    • Wisz1    Hellinga, H.W.M.S.2
  • 28
    • 0035964177 scopus 로고    scopus 로고
    • Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity
    • D.N. Bolon, and S.L. Mayo Polar residues in the protein core of Escherichia coli thioredoxin are important for fold specificity Biochemistry 40 2001 10047 10053
    • (2001) Biochemistry , vol.40 , pp. 10047-10053
    • Bolon1    Mayo, S.L.D.N.2
  • 29
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • C.D. Waldburger, J.F. Schildbach, and R.T. Sauer Are buried salt bridges important for protein stability and conformational specificity? Nat Struct Biol 2 1995 122 128
    • (1995) Nat Struct Biol , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach2    Sauer, R.T.J.F.3
  • 30
    • 0033545937 scopus 로고    scopus 로고
    • Solution structure and dynamics of a de novo designed three-helix bundle protein
    • S.T.R. Walsh, H. Cheng, J.W. Bryson, H. Roder, and W.F. DeGrado Solution structure and dynamics of a de novo designed three-helix bundle protein Proc Natl Acad Sci USA 96 1999 5486 5491
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5486-5491
    • Walsh, S.T.R.1    Cheng, H.2    Bryson, J.W.3    Roder4    Degrado, W.F.H.5
  • 31
    • 0344392714 scopus 로고    scopus 로고
    • Solution structure of a de novo protein from a designed combinatorial library
    • Y. Wei, S. Kim, D. Fela, J. Baum, and M.H. Hecht Solution structure of a de novo protein from a designed combinatorial library Proc Natl Acad Sci USA 100 2003 13270 13273 The structure of a four-helix-bundle protein identified from a combinatorial library was determined via NMR. The findings suggest that, with sufficient diversity, binary patterning of hydrophobicity consistent with secondary structure may be sufficient to obtain folding proteins.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13270-13273
    • Wei, Y.1    Kim, S.2    Fela, D.3    Baum4    Hecht, M.H.J.5
  • 32
    • 0033613164 scopus 로고    scopus 로고
    • Tanford-Kirkwood electrostatics for protein modeling
    • J.J. Havranek, and P.B. Harbury Tanford-Kirkwood electrostatics for protein modeling Proc Natl Acad Sci USA 96 1999 11145 11150
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11145-11150
    • Havranek1    Harbury, P.B.J.J.2
  • 33
    • 1942456697 scopus 로고    scopus 로고
    • Recent advances in the development and application of implicit solvent models in biomolecule simulations
    • M. Feig, and C.L. Brooks III Recent advances in the development and application of implicit solvent models in biomolecule simulations Curr Opin Struct Biol 14 2004 217 224
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 217-224
    • Brooks III, C.L.1    Feig, M.2
  • 34
    • 1842454839 scopus 로고    scopus 로고
    • Energy functions for protein design I: Efficient and accurate continuum electrostatics and solvation
    • N. Pokala, and T.M. Handel Energy functions for protein design I: efficient and accurate continuum electrostatics and solvation Protein Sci 13 2004 925 936
    • (2004) Protein Sci , vol.13 , pp. 925-936
    • Pokala1    Handel, T.M.N.2
  • 35
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • J. Desmet, M. De Maeyer, B. Hazes, and I. Lasters The dead-end elimination theorem and its use in protein side-chain positioning Nature 356 1992 539 542
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    De Maeyer, M.2    Hazes3    Lasters, I.B.4
  • 36
    • 0028212927 scopus 로고
    • Efficient rotamer elimination applied to protein side-chains and related spin glasses
    • R.F. Goldstein Efficient rotamer elimination applied to protein side-chains and related spin glasses Biophys J 66 1994 1335 1340
    • (1994) Biophys J , vol.66 , pp. 1335-1340
    • Goldstein, R.F.1
  • 37
    • 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
    • L.L. Looger, and H.W. Hellinga 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 2001 429 445
    • (2001) J Mol Biol , vol.307 , pp. 429-445
    • Looger1    Hellinga, H.W.L.L.2
  • 38
  • 39
    • 0037261324 scopus 로고    scopus 로고
    • De novo backbone and sequence design of an idealized alpha/beta-barrel protein: Evidence of stable tertiary structure
    • F. Offredi, F. Dubail, P. Kischel, K. Sarinski, A.S. Stern, C. Van de Weerdt, J.C. Hoch, C. Prosperi, J.M. Francois, and S.L. Mayo De novo backbone and sequence design of an idealized alpha/beta-barrel protein: evidence of stable tertiary structure J Mol Biol 325 2003 163 174 The authors use a DEE-based algorithm to redesign a sequence for a parameterized 216-residue TIM-barrel-like structure.
    • (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    Van De Weerdt, C.6    Hoch, J.C.7    Prosperi, C.8    Francois9    Mayo, S.L.J.M.10
  • 40
    • 0037460608 scopus 로고    scopus 로고
    • Using self-consistent fields to bias Monte Carlo methods with applications to designing and sampling protein sequences
    • J. Zou, and J.G. Saven Using self-consistent fields to bias Monte Carlo methods with applications to designing and sampling protein sequences J Chem Phys 118 2003 3843 3854
    • (2003) J Chem Phys , vol.118 , pp. 3843-3854
    • Zou1    Saven, J.G.J.2
  • 41
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • P.B. Harbury, T. Zhang, P.S. Kim, and T. Alber A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants Science 262 1993 1401 1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim3    Alber, T.P.S.4
  • 42
    • 0026532266 scopus 로고
    • Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme
    • J.H. Hurley, W.A. Baase, and B.W. Matthews Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme J Mol Biol 224 1992 1143 1159
    • (1992) J Mol Biol , vol.224 , pp. 1143-1159
    • Hurley, J.H.1    Baase2    Matthews, B.W.W.A.3
  • 43
    • 0027716138 scopus 로고
    • The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme
    • E.P. Baldwin, O. Hajiseyedjavadi, W.A. Baase, and B.W. Matthews The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme Science 262 1993 1715 1718
    • (1993) Science , vol.262 , pp. 1715-1718
    • Baldwin, E.P.1    Hajiseyedjavadi, O.2    Baase3    Matthews, B.W.W.A.4
  • 44
    • 0141524052 scopus 로고    scopus 로고
    • A de novo redesign of the WW domain
    • C.M. Kraemer-Pecore, J.T. Lecomte, and J.R. Desjarlais A de novo redesign of the WW domain Protein Sci 12 2003 2194 2205 A first example of the computational redesign of a β protein, the WW domain. The authors used their sequence prediction algorithm in combination with sampling fluctuations of the backbone in the vicinity of the target. CD and NMR measurements are consistent with the wild-type WW domain structure.
    • (2003) Protein Sci , vol.12 , pp. 2194-2205
    • Kraemer-Pecore, C.M.1    Lecomte2    Desjarlais, J.R.J.T.3
  • 46
    • 0030762021 scopus 로고    scopus 로고
    • Coupling backbone flexibility and amino acid sequence selection in protein design
    • A. Su, and S.L. Mayo Coupling backbone flexibility and amino acid sequence selection in protein design Protein Sci 6 1997 1701 1707
    • (1997) Protein Sci , vol.6 , pp. 1701-1707
    • Su1    Mayo, S.L.A.2
  • 47
    • 0035109198 scopus 로고    scopus 로고
    • Designed protein G core variants fold to native-like structures: Sequence selection by ORBIT tolerates variation in backbone specification
    • S.A. Ross, C.A. Sarisky, A. Su, and S.L. Mayo Designed protein G core variants fold to native-like structures: sequence selection by ORBIT tolerates variation in backbone specification Protein Sci 10 2001 450 454
    • (2001) Protein Sci , vol.10 , pp. 450-454
    • Ross, S.A.1    Sarisky, C.A.2    Su3    Mayo, S.L.A.4
  • 48
    • 0033516509 scopus 로고    scopus 로고
    • Side-chain and backbone flexibility in protein core design
    • J.R. Desjarlais, and T.M. Handel Side-chain and backbone flexibility in protein core design J Mol Biol 290 1999 305 318
    • (1999) J Mol Biol , vol.290 , pp. 305-318
    • Desjarlais1    Handel, T.M.J.R.2
  • 49
    • 0036667734 scopus 로고    scopus 로고
    • Combinatorial protein design
    • J.G. Saven Combinatorial protein design Curr Opin Struct Biol 12 2002 453 458
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 453-458
    • Saven, J.G.1
  • 50
    • 4143064480 scopus 로고    scopus 로고
    • Progress in the development and application of computational methods for probabilistic protein design
    • in press.
    • Park S, Kono H, Wang W, Boder ET, Saven JG: Progress in the development and application of computational methods for probabilistic protein design. Comp Chem Eng 2004, in press.
    • (2004) Comp Chem Eng
    • Park, S.1    Kono, H.2    Wang, W.3    Boder, E.T.4    Saven, J.G.5
  • 51
    • 1442335007 scopus 로고    scopus 로고
    • Probabilistic approach to the design of symmetric protein quaternary structures
    • X. Fu, H. Kono, and J.G. Saven Probabilistic approach to the design of symmetric protein quaternary structures Protein Eng 16 2003 971 977
    • (2003) Protein Eng , vol.16 , pp. 971-977
    • Fu, X.1    Kono2    Saven, J.G.H.3
  • 52
    • 1242274445 scopus 로고    scopus 로고
    • Computational design of water-soluble analogues of the potassium channel KcsA
    • A.M. Slovic, H. Kono, J.D. Lear, J.G. Saven, and W.F. DeGrado Computational design of water-soluble analogues of the potassium channel KcsA Proc Natl Acad Sci USA 101 2004 1828 1833 The successful solubilization of an integral membrane protein is presented. The designed variant retains the secondary and oligomeric structure of wild-type KcsA. Importantly, the functionally important selective binding to a scorpion toxin is retained.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1828-1833
    • Slovic, A.M.1    Kono, H.2    Lear, J.D.3    Saven4    Degrado, W.F.J.G.5
  • 53
    • 0037305504 scopus 로고    scopus 로고
    • Computational design of a water-soluble analog of phospholamban
    • A.M. Slovic, C.M. Summa, J.D. Lear, and W.F. DeGrado Computational design of a water-soluble analog of phospholamban Protein Sci 12 2003 337 348 The authors use a parameterized model structure for phospholamban and a residue-residue effective potential to identify a water-solubilized variant (WSPLB). WSPLB shares a number of experimentally determined properties with the wild-type membrane-soluble form: it is helical, possesses the same oligomerization state and is stabilized upon phosphorylation.
    • (2003) Protein Sci , vol.12 , pp. 337-348
    • Slovic, A.M.1    Summa, C.M.2    Lear3    Degrado, W.F.J.D.4
  • 54
    • 0345304457 scopus 로고    scopus 로고
    • Computational design and characterization of a monomeric helical dinuclear metalloprotein
    • J.R. Calhoun, H. Kono, S. Lahr, W. Wang, W.F. DeGrado, and J.G. Saven Computational design and characterization of a monomeric helical dinuclear metalloprotein J Mol Biol 334 2003 1101 1115 The de novo design of structure, sequence and function for a 114-residue metalloprotein is presented. The protein binds a variety of metal ions with the appropriate stoichiometry. The diiron protein exhibits catalytic activity with regard to several peroxidase substrates.
    • (2003) J Mol Biol , vol.334 , pp. 1101-1115
    • Calhoun, J.R.1    Kono, H.2    Lahr, S.3    Wang, W.4    Degrado5    Saven, J.G.W.F.6
  • 55
    • 0034612192 scopus 로고    scopus 로고
    • Retrostructural analysis of metalloproteins: Application to the design of a minimal model for diiron proteins
    • A. Lombardi, C.M. Summa, S. Geremia, L. Randaccio, V. Pavone, and W.F. DeGrado Retrostructural analysis of metalloproteins: application to the design of a minimal model for diiron proteins Proc Natl Acad Sci USA 97 2000 6298 6305
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6298-6305
    • Lombardi, A.1    Summa, C.M.2    Geremia, S.3    Randaccio, L.4    Pavone5    Degrado, W.F.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.