메뉴 건너뛰기




Volumn 20, Issue 6, 2012, Pages 1086-1096

Increasing sequence diversity with flexible backbone protein design: The complete redesign of a protein hydrophobic core

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEIN DRAA; PROTEIN DRNN; PROTEIN FBAA; UNCLASSIFIED DRUG;

EID: 84861966405     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.03.026     Document Type: Article
Times cited : (51)

References (69)
  • 1
    • 69249136329 scopus 로고    scopus 로고
    • Cluster expansion models for flexible backbone protein energetics
    • Apgar, J.R., Hahn, S., Grigoryan, G., and Keating, A.E. (2009). Cluster expansion models for flexible backbone protein energetics. J. Comput. Chem. 30, 2402-2413.
    • (2009) J. Comput. Chem. , vol.30 , pp. 2402-2413
    • Apgar, J.R.1    Hahn, S.2    Grigoryan, G.3    Keating, A.E.4
  • 2
    • 33847079676 scopus 로고    scopus 로고
    • Evaluating protein structures determined by structural genomics consortia
    • Bhattacharya, A., Tejero, R., and Montelione, G.T. (2007). Evaluating protein structures determined by structural genomics consortia. Proteins 66, 778-795.
    • (2007) Proteins , vol.66 , pp. 778-795
    • Bhattacharya, A.1    Tejero, R.2    Montelione, G.T.3
  • 3
    • 84857136656 scopus 로고    scopus 로고
    • Automated selection of stabilizing mutations in designed and natural proteins
    • Borgo, B., and Havranek, J.J. (2012). Automated selection of stabilizing mutations in designed and natural proteins. Proc. Natl. Acad. Sci. USA 109, 1494-1499.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1494-1499
    • Borgo, B.1    Havranek, J.J.2
  • 6
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C., Barber, J.D., and Barton, G.J. (2008). The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 36 (Web Server issue), 197-201.
    • (2008) Nucleic Acids Res. , vol.36 , Issue.WEB SERVER ISSUE , pp. 197-201
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3
  • 7
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999). Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 9
    • 0030987610 scopus 로고    scopus 로고
    • Probing the role of packing specificity in protein design
    • Dahiyat, B.I., and Mayo, S.L. (1997). Probing the role of packing specificity in protein design. Proc. Natl. Acad. Sci. USA 94, 10172-10177.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10172-10177
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 10
    • 0041387567 scopus 로고    scopus 로고
    • A large scale test of computational protein design: Folding and stability of nine completely redesigned globular proteins
    • Dantas, G., Kuhlman, B., Callender, D., Wong, M., and Baker, D. (2003). A large scale test of computational protein design: folding and stability of nine completely redesigned globular proteins. J. Mol. Biol. 332, 449-460.
    • (2003) J. Mol. Biol. , vol.332 , pp. 449-460
    • Dantas, G.1    Kuhlman, B.2    Callender, D.3    Wong, M.4    Baker, D.5
  • 11
    • 33846603216 scopus 로고    scopus 로고
    • High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design
    • Dantas, G., Corrent, C., Reichow, S.L., Havranek, J.J., Eletr, Z.M., Isern, N.G., Kuhlman, B., Varani,G.,Merritt, E.A., and Baker, D. (2007). High-resolution structural and thermodynamic analysis of extreme stabilization of human procarboxypeptidase by computational protein design. J. Mol. Biol. 366, 1209-1221.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1209-1221
    • Dantas, G.1    Corrent, C.2    Reichow, S.L.3    Havranek, J.J.4    Eletr, Z.M.5    Isern, N.G.6    Kuhlman, B.7    Varani, G.8    Merritt, E.A.9    Baker, D.10
  • 12
    • 3242886389 scopus 로고    scopus 로고
    • MOLPROBITY: Structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis, I.W., Murray, L.W., Richardson, J.S., and Richardson, D.C. (2004). MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32 (Web Server issue), W615-9.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.WEB SERVER ISSUE
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 13
    • 69249127027 scopus 로고    scopus 로고
    • Blind docking of pharmaceutically relevant compounds using RosettaLigand
    • Davis, I.W., Raha, K., Head, M.S., and Baker, D. (2009). Blind docking of pharmaceutically relevant compounds using RosettaLigand. Protein Sci. 18, 1998-2002.
    • (2009) Protein Sci. , vol.18 , pp. 1998-2002
    • Davis, I.W.1    Raha, K.2    Head, M.S.3    Baker, D.4
  • 14
    • 0005087945 scopus 로고    scopus 로고
    • Engineering and design Screening, selection and design: Standing at the crossroads in three dimensions
    • DeGrado, W.F., and Nilsson, B.O. (1997). Engineering and design Screening, selection and design: standing at the crossroads in three dimensions. Curr. Opin. Struct. Biol. 7, 455-456.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 455-456
    • DeGrado, W.F.1    Nilsson, B.O.2
  • 15
    • 0033516509 scopus 로고    scopus 로고
    • Side-chain and backbone flexibility in protein core design
    • Desjarlais, J.R., and Handel, T.M. (1999). Side-chain and backbone flexibility in protein core design. J. Mol. Biol. 290, 305-318.
    • (1999) J. Mol. Biol. , vol.290 , pp. 305-318
    • Desjarlais, J.R.1    Handel, T.M.2
  • 16
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K.A. (1990). Dominant forces in protein folding. Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 17
    • 0036667731 scopus 로고    scopus 로고
    • Rotamer libraries in the 21st century
    • Dunbrack, R.L., Jr. (2002). Rotamer libraries in the 21st century. Curr. Opin. Struct. Biol. 12, 431-440.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 431-440
    • Dunbrack Jr., R.L.1
  • 19
    • 45649083705 scopus 로고    scopus 로고
    • A simple model of backbone flexibility improves modeling of side-chain conformational variability
    • Friedland, G.D., Linares, A.J., Smith, C.A., and Kortemme, T. (2008). A simple model of backbone flexibility improves modeling of side-chain conformational variability. J. Mol. Biol. 380, 757-774.
    • (2008) J. Mol. Biol. , vol.380 , pp. 757-774
    • Friedland, G.D.1    Linares, A.J.2    Smith, C.A.3    Kortemme, T.4
  • 20
    • 38349008761 scopus 로고    scopus 로고
    • Toward full-sequence de novo protein design with flexible templates for human beta-defensin-2
    • Fung, H.K., Floudas, C.A., Taylor, M.S., Zhang, L., and Morikis, D. (2008). Toward full-sequence de novo protein design with flexible templates for human beta-defensin-2. Biophys. J. 94, 584-599.
    • (2008) Biophys. J. , vol.94 , pp. 584-599
    • Fung, H.K.1    Floudas, C.A.2    Taylor, M.S.3    Zhang, L.4    Morikis, D.5
  • 21
    • 34547840252 scopus 로고    scopus 로고
    • Dead-end elimination with backbone flexibility
    • Georgiev, I., and Donald, B.R. (2007). Dead-end elimination with backbone flexibility. Bioinformatics 23, i185-i194.
    • (2007) Bioinformatics , vol.23
    • Georgiev, I.1    Donald, B.R.2
  • 23
    • 79251600167 scopus 로고    scopus 로고
    • Probing designability via a generalized model of helical bundle geometry
    • Grigoryan, G., and Degrado, W.F. (2011). Probing designability via a generalized model of helical bundle geometry. J. Mol. Biol. 405, 1079-1100.
    • (2011) J. Mol. Biol. , vol.405 , pp. 1079-1100
    • Grigoryan, G.1    Degrado, W.F.2
  • 24
    • 34548764385 scopus 로고    scopus 로고
    • Computing van der Waals energies in the context of the rotamer approximation
    • Grigoryan, G., Ochoa, A., and Keating, A.E. (2007). Computing van der Waals energies in the context of the rotamer approximation. Proteins 68, 863-878.
    • (2007) Proteins , vol.68 , pp. 863-878
    • Grigoryan, G.1    Ochoa, A.2    Keating, A.E.3
  • 25
    • 0000088628 scopus 로고
    • Processing of multidimensional NMR data with the new software PROSA
    • Güntert, P., Dötsch, V., Wider, G., and Wüthrich, K. (1992). Processing of multidimensional NMR data with the new software PROSA. J. Biomol. NMR 6, 619-629.
    • (1992) J. Biomol. NMR , vol.6 , pp. 619-629
    • Güntert, P.1    Dötsch, V.2    Wider, G.3    Wüthrich, K.4
  • 26
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997). Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 27
    • 0029091449 scopus 로고
    • Repacking protein cores with backbone freedom: Structure prediction for coiled coils
    • Harbury, P.B., Tidor, B., and Kim, P.S. (1995). Repacking protein cores with backbone freedom: structure prediction for coiled coils. Proc. Natl. Acad. Sci. USA 92, 8408-8412.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8408-8412
    • Harbury, P.B.1    Tidor, B.2    Kim, P.S.3
  • 28
    • 0032553587 scopus 로고    scopus 로고
    • High-resolution protein design with backbone freedom
    • Harbury, P.B., Plecs, J.J., Tidor, B., Alber, T., and Kim, P.S. (1998). High-resolution protein design with backbone freedom. Science 282, 1462-1467.
    • (1998) Science , vol.282 , pp. 1462-1467
    • Harbury, P.B.1    Plecs, J.J.2    Tidor, B.3    Alber, T.4    Kim, P.S.5
  • 29
    • 66349133914 scopus 로고    scopus 로고
    • Motif-directed flexible backbone design of functional interactions
    • Havranek, J.J., and Baker, D. (2009). Motif-directed flexible backbone design of functional interactions. Protein Sci. 18, 1293-1305.
    • (2009) Protein Sci. , vol.18 , pp. 1293-1305
    • Havranek, J.J.1    Baker, D.2
  • 30
    • 0025040232 scopus 로고
    • De novo design, expression, and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht, M.H., Richardson, J.S., Richardson, D.C., and Ogden, R.C. (1990). De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence. Science 249, 884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 31
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002). Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 32
    • 0034657321 scopus 로고    scopus 로고
    • A polar, solvent-exposed residue can be essential for native protein structure
    • Hill, R.B., and DeGrado, W.F. (2000). A polar, solvent-exposed residue can be essential for native protein structure. Structure 8, 471-479.
    • (2000) Structure , vol.8 , pp. 471-479
    • Hill, R.B.1    DeGrado, W.F.2
  • 33
  • 34
    • 0021097529 scopus 로고
    • How good are predictions of protein secondary structure?
    • Kabsch, W., and Sander, C. (1983). How good are predictions of protein secondary structure? FEBS Lett. 155, 179-182.
    • (1983) FEBS Lett. , vol.155 , pp. 179-182
    • Kabsch, W.1    Sander, C.2
  • 35
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M., and Hecht, M.H. (1993). Protein design by binary patterning of polar and nonpolar amino acids. Science 262, 1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 37
    • 0031765187 scopus 로고    scopus 로고
    • Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effects
    • Kuhlman, B., and Raleigh, D.P. (1998). Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effects. Protein Sci. 7, 2405-2412.
    • (1998) Protein Sci. , vol.7 , pp. 2405-2412
    • Kuhlman, B.1    Raleigh, D.P.2
  • 38
    • 0034641749 scopus 로고    scopus 로고
    • Native protein sequences are close to optimal for their structures
    • Kuhlman, B., and Baker, D. (2000). Native protein sequences are close to optimal for their structures. Proc. Natl. Acad. Sci. USA 97, 10383-10388.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10383-10388
    • Kuhlman, B.1    Baker, D.2
  • 39
    • 0036300662 scopus 로고    scopus 로고
    • Accurate computer-based design of a new backbone conformation in the second turn of protein L
    • Kuhlman, B., O'Neill, J.W., Kim, D.E., Zhang, K.Y., and Baker, D. (2002). Accurate computer-based design of a new backbone conformation in the second turn of protein L. J. Mol. Biol. 315, 471-477.
    • (2002) J. Mol. Biol. , vol.315 , pp. 471-477
    • Kuhlman, B.1    O'Neill, J.W.2    Kim, D.E.3    Zhang, K.Y.4    Baker, D.5
  • 40
    • 0345306764 scopus 로고    scopus 로고
    • Design of a novel globular protein fold with atomic-level accuracy
    • Kuhlman, B., Dantas, G., Ireton, G.C., Varani, G., Stoddard, B.L., and Baker, D. (2003). Design of a novel globular protein fold with atomic-level accuracy. Science 302, 1364-1368.
    • (2003) Science , vol.302 , pp. 1364-1368
    • Kuhlman, B.1    Dantas, G.2    Ireton, G.C.3    Varani, G.4    Stoddard, B.L.5    Baker, D.6
  • 42
    • 0028147533 scopus 로고
    • The crystal structure of a mutant protein with altered but improved hydrophobic core packing
    • Lim, W.A., Hodel, A., Sauer, R.T., and Richards, F.M. (1994). The crystal structure of a mutant protein with altered but improved hydrophobic core packing. Proc. Natl. Acad. Sci. USA 91, 423-427.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 423-427
    • Lim, W.A.1    Hodel, A.2    Sauer, R.T.3    Richards, F.M.4
  • 44
  • 45
    • 0031779918 scopus 로고    scopus 로고
    • Design, structure and stability of a hyperthermophilic protein variant
    • Malakauskas, S.M., and Mayo, S.L. (1998). Design, structure and stability of a hyperthermophilic protein variant. Nat. Struct. Biol. 5, 470-475.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 470-475
    • Malakauskas, S.M.1    Mayo, S.L.2
  • 46
    • 70349775833 scopus 로고    scopus 로고
    • Backbone flexibility in computational protein design
    • Mandell, D.J., and Kortemme, T. (2009). Backbone flexibility in computational protein design. Curr. Opin. Biotechnol. 20, 420-428.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 420-428
    • Mandell, D.J.1    Kortemme, T.2
  • 48
    • 0028176595 scopus 로고
    • Measurement of the beta-sheet-forming propensities of amino acids
    • Minor, D.L., Jr., and Kim, P.S. (1994). Measurement of the beta-sheet-forming propensities of amino acids. Nature 367, 660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor Jr., D.L.1    Kim, P.S.2
  • 49
    • 0034923123 scopus 로고    scopus 로고
    • Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data
    • Moseley, H.N., Monleon, D., and Montelione, G.T. (2001). Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 339, 91-108.
    • (2001) Methods Enzymol. , vol.339 , pp. 91-108
    • Moseley, H.N.1    Monleon, D.2    Montelione, G.T.3
  • 50
    • 0030057864 scopus 로고    scopus 로고
    • What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
    • Munson, M., Balasubramanian, S., Fleming, K.G., Nagi, A.D., O'Brien, R., Sturtevant, J.M., and Regan, L. (1996). What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Sci. 5, 1584-1593.
    • (1996) Protein Sci. , vol.5 , pp. 1584-1593
    • Munson, M.1    Balasubramanian, S.2    Fleming, K.G.3    Nagi, A.D.4    O'Brien, R.5    Sturtevant, J.M.6    Regan, L.7
  • 52
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J.K., Pace, C.N., and Scholtz, J.M. (1995). Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 54
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Macromolecular Crystallography 276, 307-326.
    • (1997) Macromolecular Crystallography , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 0035782661 scopus 로고    scopus 로고
    • Review: Protein design - Where we were, where we are, where we're going
    • Pokala, N., and Handel, T.M. (2001). Review: protein design - where we were, where we are, where we're going. J. Struct. Biol. 134, 269-281.
    • (2001) J. Struct. Biol. , vol.134 , pp. 269-281
    • Pokala, N.1    Handel, T.M.2
  • 58
    • 62449335519 scopus 로고    scopus 로고
    • Protein stabilization by the rational design of surface charge-charge interactions
    • Schweiker, K.L., and Makhatadze, G.I. (2009). Protein stabilization by the rational design of surface charge-charge interactions. Methods Mol. Biol. 490, 261-283.
    • (2009) Methods Mol. Biol. , vol.490 , pp. 261-283
    • Schweiker, K.L.1    Makhatadze, G.I.2
  • 59
    • 79958079887 scopus 로고    scopus 로고
    • A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressions
    • Shapovalov, M.V., and Dunbrack, R.L., Jr. (2011). A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressions. Structure 19, 844-858.
    • (2011) Structure , vol.19 , pp. 844-858
    • Shapovalov, M.V.1    Dunbrack Jr., R.L.2
  • 60
    • 58149463441 scopus 로고    scopus 로고
    • RosettaHoles: Rapid assessment of protein core packing for structure prediction, refinement, design, and validation
    • Sheffler, W., and Baker, D. (2009). RosettaHoles: rapid assessment of protein core packing for structure prediction, refinement, design, and validation. Protein Sci. 18, 229-239.
    • (2009) Protein Sci. , vol.18 , pp. 229-239
    • Sheffler, W.1    Baker, D.2
  • 61
    • 21244479278 scopus 로고    scopus 로고
    • G-matrix Fourier transform NOESY-based protocol for high-quality protein structure determination
    • Shen, Y., Atreya, H.S., Liu, G., and Szyperski, T. (2005). G-matrix Fourier transform NOESY-based protocol for high-quality protein structure determination. J. Am. Chem. Soc. 127, 9085-9099.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9085-9099
    • Shen, Y.1    Atreya, H.S.2    Liu, G.3    Szyperski, T.4
  • 62
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M., Sawaya, M.R., Wang, S., Phillips, M., Cascio, D., and Eisenberg, D. (2006). Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103, 8060-8065.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 63
    • 0030762021 scopus 로고    scopus 로고
    • Coupling backbone flexibility and amino acid sequence selection in protein design
    • Su, A., and Mayo, S.L. (1997). Coupling backbone flexibility and amino acid sequence selection in protein design. Protein Sci. 6, 1701-1707.
    • (1997) Protein Sci. , vol.6 , pp. 1701-1707
    • Su, A.1    Mayo, S.L.2
  • 65
    • 0035846959 scopus 로고    scopus 로고
    • Hydrophobic core malleability of a de novo designed three-helix bundle protein
    • Walsh, S.T., Sukharev, V.I., Betz, S.F., Vekshin, N.L., and DeGrado, W.F. (2001). Hydrophobic core malleability of a de novo designed three-helix bundle protein. J. Mol. Biol. 305, 361-373.
    • (2001) J. Mol. Biol. , vol.305 , pp. 361-373
    • Walsh, S.T.1    Sukharev, V.I.2    Betz, S.F.3    Vekshin, N.L.4    DeGrado, W.F.5
  • 66
    • 0034477023 scopus 로고    scopus 로고
    • Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core
    • Willis, M.A., Bishop, B., Regan, L., and Brunger, A.T. (2000). Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. Structure 8, 1319-1328.
    • (2000) Structure , vol.8 , pp. 1319-1328
    • Willis, M.A.1    Bishop, B.2    Regan, L.3    Brunger, A.T.4
  • 68
    • 36749018607 scopus 로고    scopus 로고
    • Modeling backbone flexibility improves protein stability estimation
    • Yin, S., Ding, F., and Dokholyan, N.V. (2007). Modeling backbone flexibility improves protein stability estimation. Structure 15, 1567-1576.
    • (2007) Structure , vol.15 , pp. 1567-1576
    • Yin, S.1    Ding, F.2    Dokholyan, N.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.