메뉴 건너뛰기




Volumn 14, Issue 6, 2007, Pages 777-790

Hypergraph model of multi-residue interactions in proteins: Sequentially-constrained partitioning algorithms for optimization of site-directed protein recombination

Author keywords

Directed evolution; Dynamic programming; Experiment planning; Multi order residue interactions; Protein engineering

Indexed keywords

ALGORITHM; CONFERENCE PAPER; GENETIC RECOMBINATION; MATHEMATICAL ANALYSIS; MOLECULAR EVOLUTION; PRIORITY JOURNAL; PROTEIN DATABASE; PROTEIN ENGINEERING; PROTEIN INTERACTION; STATISTICAL MODEL;

EID: 34547672873     PISSN: 10665277     EISSN: None     Source Type: Journal    
DOI: 10.1089/cmb.2007.R016     Document Type: Conference Paper
Times cited : (17)

References (30)
  • 1
    • 1542323289 scopus 로고    scopus 로고
    • Staggered extension process (StEP) in vitro recombination
    • Aguinaldo, A., and Arnold, F. 2003. Staggered extension process (StEP) in vitro recombination. Methods Mol. Biol. 231, 105-110.
    • (2003) Methods Mol. Biol , vol.231 , pp. 105-110
    • Aguinaldo, A.1    Arnold, F.2
  • 2
    • 0033005899 scopus 로고    scopus 로고
    • Pair potentials for protein folding: Choice of reference states and sensitivity of predictive native states to variations in the interaction schemes
    • Betancourt, M., and Thirumalai, D. 1999. Pair potentials for protein folding: choice of reference states and sensitivity of predictive native states to variations in the interaction schemes. Protein Sci. 8, 361-369.
    • (1999) Protein Sci , vol.8 , pp. 361-369
    • Betancourt, M.1    Thirumalai, D.2
  • 3
    • 0035943455 scopus 로고    scopus 로고
    • Four-body potentials reveal protein-specific correlations to stability changes caused by hydrophobic core mutations
    • Carter, Jr., C., LeFebvre, B., Cammer, S., et al. 2001. Four-body potentials reveal protein-specific correlations to stability changes caused by hydrophobic core mutations. J. Mol. Biol. 311, 621-638.
    • (2001) J. Mol. Biol , vol.311 , pp. 621-638
    • Carter Jr., C.1    LeFebvre, B.2    Cammer, S.3
  • 4
    • 2442668927 scopus 로고    scopus 로고
    • Discovery and directed evolution of a glyphosate tolerance gene
    • Castle, L., Siehl, D., Gorton, R., et al. 2004. Discovery and directed evolution of a glyphosate tolerance gene. Science 304, 1151-1154.
    • (2004) Science , vol.304 , pp. 1151-1154
    • Castle, L.1    Siehl, D.2    Gorton, R.3
  • 5
    • 1542353447 scopus 로고    scopus 로고
    • RACHITT: Gene family shuffling by random chimeragenesis on transient templates
    • Coco, W. 2003. RACHITT: gene family shuffling by random chimeragenesis on transient templates. Methods Mol. Biol. 231, 111-127.
    • (2003) Methods Mol. Biol , vol.231 , pp. 111-127
    • Coco, W.1
  • 6
    • 9644291746 scopus 로고    scopus 로고
    • Site-directed protein recombination as a shortest-path problem
    • Endelman, J., Silberg, J., Wang, Z.-G., et al. 2004. Site-directed protein recombination as a shortest-path problem. Protein Eng. 17, 589-594.
    • (2004) Protein Eng , vol.17 , pp. 589-594
    • Endelman, J.1    Silberg, J.2    Wang, Z.-G.3
  • 7
    • 0028295169 scopus 로고
    • Correlated mutations and residue contacts in proteins
    • Gobel, U., Sander, C., Schneider, R., et al. 1994. Correlated mutations and residue contacts in proteins. Proteins 18, 309-317.
    • (1994) Proteins , vol.18 , pp. 309-317
    • Gobel, U.1    Sander, C.2    Schneider, R.3
  • 8
    • 0037271276 scopus 로고    scopus 로고
    • Fold recognition methods
    • Godzik, A. 2003. Fold recognition methods. Methods Biochem. Anal. 44, 525-546.
    • (2003) Methods Biochem. Anal , vol.44 , pp. 525-546
    • Godzik, A.1
  • 9
    • 0038799745 scopus 로고    scopus 로고
    • General method for sequence-independent site-directed chimeragenesis
    • Hiraga, K., and Arnold, F. 2003. General method for sequence-independent site-directed chimeragenesis. J. Mol. Biol. 330, 287-296.
    • (2003) J. Mol. Biol , vol.330 , pp. 287-296
    • Hiraga, K.1    Arnold, F.2
  • 10
    • 0035964191 scopus 로고    scopus 로고
    • TOUCHSTONE: An ab initio protein structure prediction method that uses threading-based tertiary restraints
    • Kihara, D., Lu, H., Kolinski, A., et al. 2001. TOUCHSTONE: an ab initio protein structure prediction method that uses threading-based tertiary restraints. Proc. Natl. Acad. Sci. USA 98, 10125-10130.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10125-10130
    • Kihara, D.1    Lu, H.2    Kolinski, A.3
  • 11
    • 0042889108 scopus 로고    scopus 로고
    • Development of a four-body statistical pseudo-potential to discriminate native from non-native protein conformations
    • Krishnamoorthy, B., and Tropsha, A. 2003. Development of a four-body statistical pseudo-potential to discriminate native from non-native protein conformations. Bioinformatics 19, 1540-1548.
    • (2003) Bioinformatics , vol.19 , pp. 1540-1548
    • Krishnamoorthy, B.1    Tropsha, A.2
  • 12
    • 0033536602 scopus 로고    scopus 로고
    • Evolutionarily conserved pathways of energetic connectivity in protein families
    • Lockless, S., and Ranganathan, R. 1999. Evolutionarily conserved pathways of energetic connectivity in protein families. Science 286, 295-299.
    • (1999) Science , vol.286 , pp. 295-299
    • Lockless, S.1    Ranganathan, R.2
  • 13
    • 0035949702 scopus 로고    scopus 로고
    • Creating multiple-crossover DNA libraries independent of sequence identity
    • Lutz, S., Ostermeier, M., Moore, G., et al. 2001. Creating multiple-crossover DNA libraries independent of sequence identity. Proc. Natl. Acad. Sci. USA 98, 11248-11253.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11248-11253
    • Lutz, S.1    Ostermeier, M.2    Moore, G.3
  • 14
    • 0026785519 scopus 로고
    • Contact potential that recognizes the correct folding of globular proteins
    • Maiorov, V., and Crippen, G. 1992. Contact potential that recognizes the correct folding of globular proteins. J. Mol. Biol. 227, 876-888.
    • (1992) J. Mol. Biol , vol.227 , pp. 876-888
    • Maiorov, V.1    Crippen, G.2
  • 15
    • 0038731100 scopus 로고    scopus 로고
    • Library analysis of SCHEMA-guided protein recombination
    • Meyer, M., Silberg, J., Voigt, C., et al. 2003. Library analysis of SCHEMA-guided protein recombination. Protein Sci. 12, 1686-1693.
    • (2003) Protein Sci , vol.12 , pp. 1686-1693
    • Meyer, M.1    Silberg, J.2    Voigt, C.3
  • 16
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S., and Jernigan, R. 1985. Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules 18, 531-552.
    • (1985) Macromolecules , vol.18 , pp. 531-552
    • Miyazawa, S.1    Jernigan, R.2
  • 17
    • 0036960601 scopus 로고    scopus 로고
    • Structure-based combinatorial protein engineering (SCOPE)
    • O'Maille, P., Bakhtina, M., and Tsai, M. 2002. Structure-based combinatorial protein engineering (SCOPE). J. Mol. Biol. 321, 677-691.
    • (2002) J. Mol. Biol , vol.321 , pp. 677-691
    • O'Maille, P.1    Bakhtina, M.2    Tsai, M.3
  • 18
    • 0037716688 scopus 로고    scopus 로고
    • Synthetic gene libraries: In search of the optimal diversity
    • Ostermeier, M. 2003. Synthetic gene libraries: in search of the optimal diversity. Trends Biotechnol. 21, 244-247.
    • (2003) Trends Biotechnol , vol.21 , pp. 244-247
    • Ostermeier, M.1
  • 19
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • Ostermeier, M., Shim, J., and Benkovic, S. 1999. A combinatorial approach to hybrid enzymes independent of DNA homology. Nature Biotechnol. 17, 1205-1209.
    • (1999) Nature Biotechnol , vol.17 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.2    Benkovic, S.3
  • 20
    • 33746268452 scopus 로고    scopus 로고
    • Site-directed combinatorial construction of chimaeric genes: General method for optimizing assembly of gene fragments
    • Saftalov, L., Smith, P., Friedman, A., et al. 2006. Site-directed combinatorial construction of chimaeric genes: general method for optimizing assembly of gene fragments. Proteins 64, 629-642.
    • (2006) Proteins , vol.64 , pp. 629-642
    • Saftalov, L.1    Smith, P.2    Friedman, A.3
  • 21
    • 24644518006 scopus 로고    scopus 로고
    • Design of combinatorial protein libraries of optimal size
    • Saraf, M.C., Gupta, A., and Maranas, C.D. 2005. Design of combinatorial protein libraries of optimal size. Proteins 60, 769-777.
    • (2005) Proteins , vol.60 , pp. 769-777
    • Saraf, M.C.1    Gupta, A.2    Maranas, C.D.3
  • 22
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber, V., Martinez, C., and Arnold, F. 2001. Libraries of hybrid proteins from distantly related sequences. Nature Biotechnol. 19, 456-460.
    • (2001) Nature Biotechnol , vol.19 , pp. 456-460
    • Sieber, V.1    Martinez, C.2    Arnold, F.3
  • 23
    • 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, K., Ruczinski, I., Kooperberg, C., et al. 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.1    Ruczinski, I.2    Kooperberg, C.3
  • 24
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons, K.T., Kooperberg, C., Huang, E., et al. 1997. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268, 209-225.
    • (1997) J. Mol. Biol , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3
  • 25
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force, an approach to the knowledge-based prediction of local structures in globular proteins
    • Sippl, M. 1990. Calculation of conformational ensembles from potentials of mean force, an approach to the knowledge-based prediction of local structures in globular proteins. J. Mol. Biol. 213, 859-883.
    • (1990) J. Mol. Biol , vol.213 , pp. 859-883
    • Sippl, M.1
  • 26
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. 1994. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370, 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.1
  • 27
    • 0017021957 scopus 로고
    • Medium and long range interaction parameters between amino acids for predicting three dimensional structures of proteins
    • Tanaka, S., and Scheraga, H. 1976. Medium and long range interaction parameters between amino acids for predicting three dimensional structures of proteins. Macromolecules 9, 945-950.
    • (1976) Macromolecules , vol.9 , pp. 945-950
    • Tanaka, S.1    Scheraga, H.2
  • 29
    • 0036289574 scopus 로고    scopus 로고
    • Protein building blocks preserved by recombination
    • Voigt, C., Martinez, C., Wang, Z., et al. 2002. Protein building blocks preserved by recombination. Nature Struct. Biol. 9, 553-558.
    • (2002) Nature Struct. Biol , vol.9 , pp. 553-558
    • Voigt, C.1    Martinez, C.2    Wang, Z.3
  • 30
    • 0043180474 scopus 로고    scopus 로고
    • Pisces: A protein sequence culling server
    • Wang, G., and Dunbrack Jr., R.L. 2003. Pisces: a protein sequence culling server. Bioinformatics 19, 1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack Jr., R.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.