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 REFERENCES
Note: OCR errors may be found in this Reference List extracted from the full text article. ACM has opted to expose the complete List rather than only correct and linked references.
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Bryant, S. H. & Lawrence, C. E. (1993). An empirical energy function for threading protein sequence through folding motif. Proteins: Struct. Funct. Genet. 16, 92-112.
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2
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Chiu T. & Goldstein, R. A. (1998). Optimizing energy potentials for success in protein tertiary structure prediction. Folding & Design 3, 223-228.
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3
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Colonna-Cesari, F. & Sander, C. (1990). Excluded volume approximation to protein-solvent interaction. The solvent contact model. Biophys. J. 57, 1103-1107.
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4
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Crippen, G. M. (1991). Prediction of protein folding from amino acid sequence over discrete conformation space. Biochemistry, 30, 4232-4237.
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5
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Dumont, M. E., Corin, A. E & Campbell, G. A. (1994). Noncovalent binding of heine induces a compact apocytochrome c structure. Biochemistry 33, 7368- 7378.
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6
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Goldstein, R. A., Luthey-Schulten, Z. A. & Wolynes, P. G. (1992). Protein tertiary structure recognition using optimized hamiltonians with local interactions. Proc. Natl. Acad. Sci. USA 89, 9029-9033.
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7
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Hendlich, M., Lackner, P., Weitckus, S., Floeckner, H., Froschauer, R., Gottsbaeher, Casari, G. & Sippl, M. J. (1990). identification of native protein folds amongst a large number of incorrect models. The calculation of low energy conformations from potentials of mean force. J. Mol. Biol. 216, 167-180.
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8
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Hobohm, U., Scharf, M., Schneider, R. & Sander, C. (1992). Selection of a representative set of structures from the Brookhaven Protein Data Bank. Protein Science 1,409-417.
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9
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Huang, E. S., Subbiah, S. & Levitt, M. (1995). Recognizing native folds by the arrangement of hydrophobic and polar residues. J. Mol. Biol. 252, 709-720.
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Huang, E. S., Subbiah, S., Tsai, J. & Levitt, M. (1996). a Hydrophobie Contact Potential to Evaluate Native and Near-native Folds Generated by Moleculax Dynamics Simulations. J. Mol. Biol. 257, 716- 725.
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11
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Huber, T. & Torda, A. E. (1998). Protein fold recognition without Boltzmann statistics or explicit physical basis. Protein Science 7, 142-149.
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12
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Jones, D. T. (1997). Progress in protein structure prediction. Curr. Op. in Struct. Biol. 7, 377-387.
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13
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Maiorov, V. N. & Crippen, G. M. (1992). Contact potential recognizes the correct folding of globular proteins. J. Mol. Biol. 227, 876-888.
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14
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Miyazawa, S. & Jemigan, R. L. (1985). Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules, 18, 534-552.
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15
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Miyazawa, S. & Jemigan, R. L. (1996). Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. J. Mol. Biol. 256, 623-644.
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16
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Park, B. & Levitt, M. (1996). Energy Functions that Discriminate X-ray and Near-native Folds from Wellconstructed Decoys. J. Mol. Biol. 258, 367-392.
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17
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Park, B. H., Huang, E. S. & Levitt, M. (1997). Factors Affecting the Ability of Energy Functions to Discriminate Correct from Incorrect Folds. J. Mol. Biol. 266, 831-846.
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18
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Reva, B. A., Finkelstein, A. V. & Skolnick, J. (1998). What is the probability of a chance prediction of a protein structure with an rmsd of 6 ,/t? Folding & Design 3, 141-147.
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19
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Sippl, M. J. (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.
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20
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Thomas, P. D. & Dill, K. A. (1996). Statistical potentials extracted from protein structures: how accurate are they? J. Mol. Biol. 257, 457-469.
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