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Volumn 258, Issue 1, 1996, Pages 201-209

From structure to sequence and back again

Author keywords

Conformational search; Inverse folding; Lattice model; Protein design

Indexed keywords

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0029883960     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0243     Document Type: Article
Times cited : (33)

References (23)
  • 1
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie, J. U., Luthy, R. & Eisenberg, D. (1991). A method to identify protein sequences that fold into a known three-dimensional structure. Science, 253, 164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 2
    • 0027318781 scopus 로고
    • Kinetics and thermodynamics of folding in model proteins
    • Camacho, C. J. & Thirumalai, D. (1993). Kinetics and thermodynamics of folding in model proteins. Proc. Natl Acad. Sci. USA, 90, 6369-6372.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6369-6372
    • Camacho, C.J.1    Thirumalai, D.2
  • 3
    • 0026418178 scopus 로고
    • A search for the most stable folds of protein chains
    • Finkelstein, A. V. & Reva, B. A. (1991). A search for the most stable folds of protein chains. Nature, 351, 497-499.
    • (1991) Nature , vol.351 , pp. 497-499
    • Finkelstein, A.V.1    Reva, B.A.2
  • 4
    • 0026726481 scopus 로고
    • Topology fingerprint approach to the inverse protein folding problem
    • Godzik, A., Kolinski, A. & Skolnick, J. (1992). Topology fingerprint approach to the inverse protein folding problem. J. Mol. Biol. 227, 227-238.
    • (1992) J. Mol. Biol. , vol.227 , pp. 227-238
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 6
    • 0028237287 scopus 로고
    • Optimal sequence selection in proteins of known structure by simulated evolution
    • Hellinga, H. W. & Richards, F. M. (1994). Optimal sequence selection in proteins of known structure by simulated evolution. Proc. Natl Acad. Sci. USA, 91, 5803-5807.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5803-5807
    • Hellinga, H.W.1    Richards, F.M.2
  • 7
    • 0026519315 scopus 로고
    • A lattice model for protein structure prediction at low resolution
    • Hinds, D. A. & Levitt, M. (1992). A lattice model for protein structure prediction at low resolution. Proc. Natl Acad. Sci. USA, 89, 2536-2540.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2536-2540
    • Hinds, D.A.1    Levitt, M.2
  • 8
    • 0028149160 scopus 로고
    • Exploring conformational space with a simple lattice model for protein structure
    • Hinds, D. A. & Levitt, M. (1994). Exploring conformational space with a simple lattice model for protein structure. J. Mol. Biol. 243, 668-682.
    • (1994) J. Mol. Biol. , vol.243 , pp. 668-682
    • Hinds, D.A.1    Levitt, M.2
  • 10
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of proteins
    • Lau, K. T. & Dill, K. A. (1989). A lattice statistical mechanics model of the conformational and sequence spaces of proteins. Macromolecules, 22, 3986-3997.
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.T.1    Dill, K.A.2
  • 11
    • 0025101549 scopus 로고
    • Theory for protein mutability and biogenesis
    • Lau, K. T. & Dill, K. A. (1990). Theory for protein mutability and biogenesis. Proc. Natl Acad. Sci. USA, 87, 638-642.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 638-642
    • Lau, K.T.1    Dill, K.A.2
  • 12
    • 0023644998 scopus 로고
    • Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 Å
    • Leijonmarck, M. & Liljas, A. (1987). Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 Å. J. Mol. Biol. 195, 555-580.
    • (1987) J. Mol. Biol. , vol.195 , pp. 555-580
    • Leijonmarck, M.1    Liljas, A.2
  • 13
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • Miyazawa, S. & Jernigan, R. L. (1985). Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules, 18, 534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 14
    • 0021108287 scopus 로고
    • Designing proteins and peptides
    • Pabo, C. (1983). Designing proteins and peptides. Nature, 301, 200.
    • (1983) Nature , vol.301 , pp. 200
    • Pabo, C.1
  • 15
    • 0029063717 scopus 로고
    • The complexity and accuracy of discrete state models of protein structure
    • Park, B. H. & Levitt, M. (1995). The complexity and accuracy of discrete state models of protein structure. J. Mol. Biol. 249, 493-507.
    • (1995) J. Mol. Biol. , vol.249 , pp. 493-507
    • Park, B.H.1    Levitt, M.2
  • 16
    • 0023155210 scopus 로고
    • Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different stuctural classes
    • Ponder, J. W. & Richards, F. M. (1987). Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different stuctural classes. J. Mol. Biol. 193, 775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 17
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • Sali, A., Shakhnovich, E. & Karplus, M. (1994). Kinetics of protein folding: a lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235, 1614-1636.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 18
    • 0027234766 scopus 로고
    • Engineering of stable and fast-folding sequences of model proteins
    • Shakhnovich, E. I. & Gutin, A. M. (1993). Engineering of stable and fast-folding sequences of model proteins. Proc. Natl Acad. Sci. USA, 90, 7195-7199.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7195-7199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 19
    • 0000903215 scopus 로고
    • A method for predicting protein structure from sequence
    • Skolnick, J., Kolinski, A., Brooks, C. L. & Rey, A. (1993). A method for predicting protein structure from sequence. Curr Biol. 3, 414-423.
    • (1993) Curr Biol. , vol.3 , pp. 414-423
    • Skolnick, J.1    Kolinski, A.2    Brooks, C.L.3    Rey, A.4
  • 20
    • 0027458885 scopus 로고
    • Three-dimensional profiles from residue-pair preferences: Identification of sequences with β/α-barrel fold
    • Wilmanns, M. & Eisenberg, D. (1993). Three-dimensional profiles from residue-pair preferences: identification of sequences with β/α-barrel fold. Proc. Natl Acad. Sci. USA, 90, 1379-1383.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1379-1383
    • Wilmanns, M.1    Eisenberg, D.2
  • 21
    • 0026582243 scopus 로고
    • Inverse protein folding problem: Designing polymer sequences
    • Yue, K. & Dill, K. A. (1992). Inverse protein folding problem: designing polymer sequences. Proc. Natl Acad. Sci. USA, 89, 4163-4167.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4163-4167
    • Yue, K.1    Dill, K.A.2
  • 22
    • 0028950075 scopus 로고
    • Forces of tertiary structural organization in globular proteins
    • Yue, K. & Dill, K. A. (1995). Forces of tertiary structural organization in globular proteins. Proc. Natl Acad. Sci. USA, 92, 146-150.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 146-150
    • Yue, K.1    Dill, K.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.