메뉴 건너뛰기




Volumn 7, Issue 11, 1998, Pages 2287-2300

Determinants of strand register in antiparallel β-sheets of proteins

Author keywords

Aromatic aromatic interactions; Aromatic peptide interactions; Profile analysis; Protein design; Protein folding; Protein modeling; Protein structure; Strand; structure

Indexed keywords

AMINO ACID; PROTEIN;

EID: 0031735020     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560071106     Document Type: Article
Times cited : (167)

References (69)
  • 1
    • 0015859467 scopus 로고
    • Principles thai govern the folding of protein chains
    • Anfinsen CB. 1973. Principles thai govern the folding of protein chains. Science 181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0029154811 scopus 로고
    • Native-like and structurally characterized designed alpha-helical bundles
    • Betz SF, Bryson JW, Degrado WF. 1995. Native-like and structurally characterized designed alpha-helical bundles. Curr Opin Struct Biol 5:457-463.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 457-463
    • Betz, S.F.1    Bryson, J.W.2    Degrado, W.F.3
  • 4
    • 0027249641 scopus 로고
    • De-novo protein design - From molten globules to native-like states
    • Betz SF, Raleigh DP, Degrado WF. 1993. De-novo protein design - From molten globules to native-like states. Curr Opin Struct Biol 3:601-610.
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 601-610
    • Betz, S.F.1    Raleigh, D.P.2    Degrado, W.F.3
  • 7
    • 0024260626 scopus 로고
    • Weakly polar interactions in proteins
    • Burley SK, Petsko GA. 1988. Weakly polar interactions in proteins. Adv Protein Chem 39:125-189.
    • (1988) Adv Protein Chem , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 8
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, beta-sheet and random coil regions calculated from proteins
    • Chou PY, Fasman GD. 1974. Conformational parameters for amino acids in helical, beta-sheet and random coil regions calculated from proteins. Biochemistry 13:211-222.
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 9
    • 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
  • 10
    • 1842403587 scopus 로고    scopus 로고
    • Turn residue sequence determines beta-hairpin conformation in designed peptides
    • de Alba E, Angeles-Jiménez M, Rico M. 1997a. Turn residue sequence determines beta-hairpin conformation in designed peptides. J Am Chem Soc 119:175-183.
    • (1997) J Am Chem Soc , vol.119 , pp. 175-183
    • De Alba, E.1    Angeles-Jiménez, M.2    Rico, M.3
  • 11
    • 0030334822 scopus 로고    scopus 로고
    • Conformational investigation of designed short linear peptides able to fold into beta-hairpin structures in aqueous solution
    • de Alba E, Angeles-Jimémez M, Rico M, Nieto JL. 1996. Conformational investigation of designed short linear peptides able to fold into beta-hairpin structures in aqueous solution. Fold Design 1:133-144.
    • (1996) Fold Design , vol.1 , pp. 133-144
    • De Alba, E.1    Angeles-Jimémez, M.2    Rico, M.3    Nieto, J.L.4
  • 12
    • 0031454065 scopus 로고    scopus 로고
    • Cross-strand side-chain interactions versus turn conformation in β-hairpins
    • de Alba E, Rico M, Angeles-Jiménez M. 1997b. Cross-strand side-chain interactions versus turn conformation in β-hairpins. Protein Sci 6:2548-2560.
    • (1997) Protein Sci , vol.6 , pp. 2548-2560
    • De Alba, E.1    Rico, M.2    Angeles-Jiménez, M.3
  • 13
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 14
    • 0028961135 scopus 로고
    • Predicted beta-structure stability parameters under experimental test
    • Finkelstein AV. 1995. Predicted beta-structure stability parameters under experimental test. Protein Eng 8:207-209.
    • (1995) Protein Eng , vol.8 , pp. 207-209
    • Finkelstein, A.V.1
  • 15
    • 0029996162 scopus 로고    scopus 로고
    • Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence
    • Frishman D, Argos P. 1996. Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence. Protein Eng 9:133-142.
    • (1996) Protein Eng , vol.9 , pp. 133-142
    • Frishman, D.1    Argos, P.2
  • 16
    • 16944366990 scopus 로고    scopus 로고
    • Buried polar residues and structural specificity in the GCN4 leucine-zipper
    • Gonzalez LJ, Woolfson DN, Alber T. 1996. Buried polar residues and structural specificity in the GCN4 leucine-zipper. Nature Struct Biol 3:1011-1018.
    • (1996) Nature Struct Biol , vol.3 , pp. 1011-1018
    • Gonzalez, L.J.1    Woolfson, D.N.2    Alber, T.3
  • 17
    • 0031455857 scopus 로고    scopus 로고
    • Beta-hairpins in proteins revisited: Lessons for de novo design
    • Gunasekaran K, Ramakrishnan C, Balaram P. 1997. Beta-hairpins in proteins revisited: Lessons for de novo design. Protein Eng 10:1131-1141.
    • (1997) Protein Eng , vol.10 , pp. 1131-1141
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 18
    • 0027756896 scopus 로고
    • A switch between 2-stranded, 3-stranded and 4-stranded coiled coils in GCN4 leucine-zipper mutants
    • Harbury PB, Zhang T, Kim PS, Alber T. 1993. A switch between 2-stranded, 3-stranded and 4-stranded coiled coils in GCN4 leucine-zipper mutants. Science 262:1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 19
    • 0344900077 scopus 로고
    • NMR shifts in aromatic solvents
    • Hatton JV, Richards RE. 1962a. NMR shifts in aromatic solvents. Mol Phys 5:153-159.
    • (1962) Mol Phys , vol.5 , pp. 153-159
    • Hatton, J.V.1    Richards, R.E.2
  • 20
    • 0009474016 scopus 로고
    • Solvent effects in NMR spectra of amide solutions
    • Hatton JV, Richards RE. 1962b. Solvent effects in NMR spectra of amide solutions. Mol Phys 5:139-152.
    • (1962) Mol Phys , vol.5 , pp. 139-152
    • Hatton, J.V.1    Richards, R.E.2
  • 21
    • 0027500954 scopus 로고
    • Rational design and binding of modified cell-wall peptides to vancomycin-group antibiotics-factorizing free-energy contributions to binding
    • Holroyd SE, Groves P, Searle MS, Gerhard U, Williams DH. 1993. Rational design and binding of modified cell-wall peptides to vancomycin-group antibiotics-factorizing free-energy contributions to binding. Tetrahedron 49:9171-9182.
    • (1993) Tetrahedron , vol.49 , pp. 9171-9182
    • Holroyd, S.E.1    Groves, P.2    Searle, M.S.3    Gerhard, U.4    Williams, D.H.5
  • 22
    • 0029101826 scopus 로고
    • Recognizing native folds by the arrangement of hydrophobic and polar residues
    • Huang ES, Subbiah S, Levitt M. 1995. Recognizing native folds by the arrangement of hydrophobic and polar residues. J Mol Biol 252:709-720.
    • (1995) J Mol Biol , vol.252 , pp. 709-720
    • Huang, E.S.1    Subbiah, S.2    Levitt, M.3
  • 23
    • 0028874810 scopus 로고
    • Fold recognition and ab-initio structure predictions using hidden markov-models and beta-strand pair potentials
    • Hubbard TJ, Park J. 1995. Fold recognition and ab-initio structure predictions using hidden markov-models and beta-strand pair potentials. Proteins Struct Funct Genet 23:398-402.
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 398-402
    • Hubbard, T.J.1    Park, J.2
  • 24
    • 0001227655 scopus 로고
    • The nature of π-π interactions
    • Hunter CA, Sanders JKM. 1990. The nature of π-π interactions. J Am Chem Soc 112:5525-5534.
    • (1990) J Am Chem Soc , vol.112 , pp. 5525-5534
    • Hunter, C.A.1    Sanders, J.K.M.2
  • 25
    • 0025878347 scopus 로고
    • π-π-interactions - The geometry and energetics of phenylalanine-phenylalanine interactions in proteins
    • Hunter CA, Singh J, Thornton JM. 1991. π-π-interactions - The geometry and energetics of phenylalanine-phenylalanine interactions in proteins. J Mol Biol 218:837-846.
    • (1991) J Mol Biol , vol.218 , pp. 837-846
    • Hunter, C.A.1    Singh, J.2    Thornton, J.M.3
  • 26
    • 0028882032 scopus 로고
    • Measuring the strength of side-chain hydrogen bonds in peptide helices - The Gln-center-dot-Asp-(i,i + 4) interaction
    • Huyghues-Despointes BMP, Klingler TM, Baldwin RL. 1995. Measuring the strength of side-chain hydrogen bonds in peptide helices - The Gln-center-dot-Asp-(i,i + 4) interaction. Biochemistry 34:13267-13271.
    • (1995) Biochemistry , vol.34 , pp. 13267-13271
    • Huyghues-Despointes, B.M.P.1    Klingler, T.M.2    Baldwin, R.L.3
  • 27
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure - Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W, Sander C. 1983. Dictionary of protein secondary structure - Pattern recognition of hydrogen bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0028878268 scopus 로고
    • The physical properties of local interactions of tyrosine residues in peptides and unfolded proteins
    • Kemmink J, Creighton TE. 1995. The physical properties of local interactions of tyrosine residues in peptides and unfolded proteins. J Mol Biol 245:251-260.
    • (1995) J Mol Biol , vol.245 , pp. 251-260
    • Kemmink, J.1    Creighton, T.E.2
  • 29
    • 0027398888 scopus 로고
    • Local-structure due to an aromatic amide interaction observed by H-1-nuclear magnetic-resonance spectroscopy in peptides related to the n terminus of bovine pancreatic trypsin-inhibitor
    • Kemmink J, Vanmierlo CPM, Scheck RM, Creighton TE. 1993. Local-structure due to an aromatic amide interaction observed by H-1-nuclear magnetic-resonance spectroscopy in peptides related to the n terminus of bovine pancreatic trypsin-inhibitor. J Mol Biol 230:312-322.
    • (1993) J Mol Biol , vol.230 , pp. 312-322
    • Kemmink, J.1    Vanmierlo, C.P.M.2    Scheck, R.M.3    Creighton, T.E.4
  • 30
    • 0025484611 scopus 로고
    • Peptidomimetics and the template approach to nucleation of beta-sheets and alpha-helices in peptides
    • Kemp DS. 1990. Peptidomimetics and the template approach to nucleation of beta-sheets and alpha-helices in peptides. Trends in Biotechnology 8:249-255.
    • (1990) Trends in Biotechnology , vol.8 , pp. 249-255
    • Kemp, D.S.1
  • 31
    • 0025079448 scopus 로고
    • Synthesis and conformational-analysis of epindolidione-derived peptide models for beta-sheet formation
    • Kemp DS, Bowen BR, Muendel CC. 1990. Synthesis and conformational-analysis of epindolidione-derived peptide models for beta-sheet formation. J Organic Chem 55:4650-4657.
    • (1990) J Organic Chem , vol.55 , pp. 4650-4657
    • Kemp, D.S.1    Bowen, B.R.2    Muendel, C.C.3
  • 32
    • 0027411181 scopus 로고
    • Thermodynamic beta-sheet propensities measured using a zinc finger host peptide
    • Kim CA, Berg JM. 1993. Thermodynamic beta-sheet propensities measured using a zinc finger host peptide. Nature 362:267-270.
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: Program to check the stereochemical quality of protein structures
    • Laskowski RA, Mac-Arthur MW, Moss DS, Thornton JM. 1993. PROCHECK: Program to check the stereochemical quality of protein structures. J App Cryst 26:283-291.
    • (1993) J App Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Mac-Arthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • Lazar GA, Desjarlais JR, Handel TM. 1997. De novo design of the hydrophobic core of ubiquitin. Protein Sci 6:1167-1178.
    • (1997) Protein Sci , vol.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 35
    • 0018093765 scopus 로고
    • Conformational preferences for amino acids in globular proteins
    • Levitt M. 1978. Conformational preferences for amino acids in globular proteins. Biochemistry 17:4277-4285.
    • (1978) Biochemistry , vol.17 , pp. 4277-4285
    • Levitt, M.1
  • 36
    • 0019317336 scopus 로고
    • Specific recognition in the tertiary structure of β-sheets of proteins
    • Lifson S, Sander C. 1980. Specific recognition in the tertiary structure of β-sheets of proteins. J Mol Biol 139:627-639.
    • (1980) J Mol Biol , vol.139 , pp. 627-639
    • Lifson, S.1    Sander, C.2
  • 37
    • 0016162558 scopus 로고
    • Algorithms for prediction of a-helical and β-structural regions of globular proteins
    • Lim VI. 1974a. Algorithms for prediction of a-helical and β-structural regions of globular proteins. J Mol Biol 88:873-894.
    • (1974) J Mol Biol , vol.88 , pp. 873-894
    • Lim, V.I.1
  • 38
    • 0016209912 scopus 로고
    • Structural principles of the globular organization of protein chains: A stereochemical theory of globular protein secondary structure
    • Lim VI. 1974b. Structural principles of the globular organization of protein chains: A stereochemical theory of globular protein secondary structure. J Mol Biol 88:857-872.
    • (1974) J Mol Biol , vol.88 , pp. 857-872
    • Lim, V.I.1
  • 39
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • McGregor MJ, Islam SA, Sternberg MJ. 1987. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J Mol Biol 198:295-310.
    • (1987) J Mol Biol , vol.198 , pp. 295-310
    • McGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.3
  • 40
    • 0028176595 scopus 로고
    • Measurement of the beta-sheet-forming propensities of amino acids
    • Minor DL, Kim PS. 1994a. Measurement of the beta-sheet-forming propensities of amino acids. Nature 367:660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor, D.L.1    Kim, P.S.2
  • 41
    • 0027998757 scopus 로고
    • Context is a major determinant of beta-sheet propensity
    • Minor DL, Kim PS. 1994b. Context is a major determinant of beta-sheet propensity. Nature 371:264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor, D.L.1    Kim, P.S.2
  • 42
    • 0028301445 scopus 로고
    • Amino/aromatic interactions in proteins - Is the evidence stacked against hydrogen-bonding?
    • Mitchell JBO, Nandi CL, McDonald IK, Thornton JM, Price SL. 1994, Amino/aromatic interactions in proteins - Is the evidence stacked against hydrogen-bonding? J Mol Biol 239-315-331.
    • (1994) J Mol Biol , vol.239 , pp. 315-331
    • Mitchell, J.B.O.1    Nandi, C.L.2    McDonald, I.K.3    Thornton, J.M.4    Price, S.L.5
  • 43
    • 0028568650 scopus 로고
    • Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices - Comparison with experimental scales
    • Muñoz V, Serrano L. 1994. Intrinsic secondary structure propensities of the amino acids, using statistical phi-psi matrices - Comparison with experimental scales. Proteins Struct Fund Genet 20:301-311.
    • (1994) Proteins Struct Fund Genet , vol.20 , pp. 301-311
    • Muñoz, V.1    Serrano, L.2
  • 45
    • 0030627165 scopus 로고    scopus 로고
    • Local interactions of aromatic residues in short peptides in aqueous solution: A combined database and energetic analysis
    • Nardi F, Worth GA, Wade RC. 1997. Local interactions of aromatic residues in short peptides in aqueous solution: A combined database and energetic analysis. Fold Design 2:S62-S68.
    • (1997) Fold Design , vol.2
    • Nardi, F.1    Worth, G.A.2    Wade, R.C.3
  • 46
    • 0026759751 scopus 로고
    • Fast structure alignment for protein databank searching
    • Orengo CA, Brown NP, Taylor WR. 1992. Fast structure alignment for protein databank searching. Proteins 14:139-167.
    • (1992) Proteins , vol.14 , pp. 139-167
    • Orengo, C.A.1    Brown, N.P.2    Taylor, W.R.3
  • 47
    • 0028988836 scopus 로고
    • Side-chain determinants of beta-sheet stability
    • Otzen DE, Fersht AR. 1995. Side-chain determinants of beta-sheet stability. Biochemistry 34:5718-5724.
    • (1995) Biochemistry , vol.34 , pp. 5718-5724
    • Otzen, D.E.1    Fersht, A.R.2
  • 48
    • 0027968834 scopus 로고
    • Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i,i + 4
    • Padmanabhan S, Baldwin RL. 1994a. Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i,i + 4. J Mol Biol 241:706-713.
    • (1994) J Mol Biol , vol.241 , pp. 706-713
    • Padmanabhan, S.1    Baldwin, R.L.2
  • 49
    • 0028569692 scopus 로고
    • Tests for helix-stabilizing interactions between various nonpolar side-chains in alanine-based peptides
    • Padmanabhan S, Baldwin RL. 1994b. Tests for helix-stabilizing interactions between various nonpolar side-chains in alanine-based peptides. Protein Sci 3:1992-1997.
    • (1994) Protein Sci , vol.3 , pp. 1992-1997
    • Padmanabhan, S.1    Baldwin, R.L.2
  • 50
    • 0031885491 scopus 로고    scopus 로고
    • A stable single layer beta-sheet without a hydrophobic core
    • Pham TN, Koide A, Koide S. 1998. A stable single layer beta-sheet without a hydrophobic core. Nature Struct Biol 5:115-119.
    • (1998) Nature Struct Biol , vol.5 , pp. 115-119
    • Pham, T.N.1    Koide, A.2    Koide, S.3
  • 51
    • 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 193:775-791.
    • (1987) J Mol Biol , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, F.M.2
  • 52
    • 79954515341 scopus 로고
    • A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state
    • Raleigh DP, DeGrado WF. 1992. A de novo designed protein shows a thermally induced transition from a native to a molten globule-like state. J Am Chem Soc 114:10079-10081.
    • (1992) J Am Chem Soc , vol.114 , pp. 10079-10081
    • Raleigh, D.P.1    DeGrado, W.F.2
  • 53
    • 0031558811 scopus 로고    scopus 로고
    • Role of beta-turn residues in beta-hairpin formation and stability in designed peptides
    • Ramirez-Alvarado M, Blanco FJ, Niemann H, Serrano L. 1997. Role of beta-turn residues in beta-hairpin formation and stability in designed peptides. J Mol Biol 273:898-912.
    • (1997) J Mol Biol , vol.273 , pp. 898-912
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Niemann, H.3    Serrano, L.4
  • 54
    • 0029891313 scopus 로고    scopus 로고
    • De-novo design and structural-analysis of a model beta-hairpin peptide system
    • Ramirez-Alvarado M, Blanco FJ, Serrano L. 1996. De-novo design and structural-analysis of a model beta-hairpin peptide system. Nature Struct Biol 3:604-612.
    • (1996) Nature Struct Biol , vol.3 , pp. 604-612
    • Ramirez-Alvarado, M.1    Blanco, F.J.2    Serrano, L.3
  • 55
    • 0030878180 scopus 로고    scopus 로고
    • A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties
    • Roy S, Ratnaswamy G, Boice JA, Fairman R, McLendon G, Hecht MH. 1997. A protein designed by binary patterning of polar and nonpolar amino acids displays native-like properties. J Am Chem Soc 119:5302-5306.
    • (1997) J Am Chem Soc , vol.119 , pp. 5302-5306
    • Roy, S.1    Ratnaswamy, G.2    Boice, J.A.3    Fairman, R.4    McLendon, G.5    Hecht, M.H.6
  • 57
    • 0028865129 scopus 로고
    • A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin
    • Searle MS, Williams DH, Packman LC. 1995. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native beta-hairpin. Nature Struct Biol 2:999-1006.
    • (1995) Nature Struct Biol , vol.2 , pp. 999-1006
    • Searle, M.S.1    Williams, D.H.2    Packman, L.C.3
  • 59
    • 0028792105 scopus 로고
    • Guidelines for protein design - The energetics of beta-sheet side-chain interactions
    • Smith CK, Regan L. 1995. Guidelines for protein design - The energetics of beta-sheet side-chain interactions. Science 270:980-982.
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 60
    • 0028175780 scopus 로고
    • A thermodynamic scale for the beta-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L. 1994. A thermodynamic scale for the beta-sheet forming tendencies of the amino acids. Biochemistry 33:5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 61
    • 0031587297 scopus 로고    scopus 로고
    • Hydrogen bonding interactions between glutamine and asparagine in α-helical peptides
    • Stapley BJ, Doig AJ. 1997. Hydrogen bonding interactions between glutamine and asparagine in α-helical peptides. J Mol Biol 272:465-473.
    • (1997) J Mol Biol , vol.272 , pp. 465-473
    • Stapley, B.J.1    Doig, A.J.2
  • 62
    • 0028841399 scopus 로고
    • A simple protein-folding algorithm using a binary code and secondary structure constraints
    • Sun SJ, Thomas PD, Dill KA. 1995. A simple protein-folding algorithm using a binary code and secondary structure constraints. Protein Eng 8:769-778.
    • (1995) Protein Eng , vol.8 , pp. 769-778
    • Sun, S.J.1    Thomas, P.D.2    Dill, K.A.3
  • 63
    • 0029147823 scopus 로고
    • Intrinsic phi,psi propensities of amino acids, derived from the coil regions of known structures
    • Swindells MB, MacArthur MW, Thornton JM. 1995. Intrinsic phi,psi propensities of amino acids, derived from the coil regions of known structures. Nature Struct Biol 2:596-603.
    • (1995) Nature Struct Biol , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 64
    • 0029070109 scopus 로고
    • Conserved structural features on protein surfaces -Small exterior hydrophobic clusters
    • Tisi LC, Evans PA. 1995. Conserved structural features on protein surfaces -Small exterior hydrophobic clusters. J Mol Biol 249:251-258.
    • (1995) J Mol Biol , vol.249 , pp. 251-258
    • Tisi, L.C.1    Evans, P.A.2
  • 66
    • 0028846974 scopus 로고
    • Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins
    • West MW, Hecht MH. 1995. Binary patterning of polar and nonpolar amino acids in the sequences and structures of native proteins. Protein Sci 4:2032-2039.
    • (1995) Protein Sci , vol.4 , pp. 2032-2039
    • West, M.W.1    Hecht, M.H.2
  • 67
    • 0029083811 scopus 로고
    • Predicting oligomerization states of coiled coils
    • Woolfson DN, Alber T. 1995. Predicting oligomerization states of coiled coils. Protein Sci 4:1596-1607.
    • (1995) Protein Sci , vol.4 , pp. 1596-1607
    • Woolfson, D.N.1    Alber, T.2
  • 68
    • 5844406560 scopus 로고
    • The aromatic-(i + 2) amine interaction in peptides
    • Worth GA, Wade RC. 1995. The aromatic-(i + 2) amine interaction in peptides. J Phys Chem 99:17473-17482.
    • (1995) J Phys Chem , vol.99 , pp. 17473-17482
    • Worth, G.A.1    Wade, R.C.2
  • 69
    • 0029058159 scopus 로고
    • An analysis of side-chain interactions and pair correlations within antiparallel beta-sheets: The differences between backbone hydrogen bonded and non-hydrogen-bonded residue pairs
    • Wouters MA, Curmi PMG. 1995. An analysis of side-chain interactions and pair correlations within antiparallel beta-sheets: The differences between backbone hydrogen bonded and non-hydrogen-bonded residue pairs. Proteins 22:119-131.
    • (1995) Proteins , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.