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Volumn 47, Issue 4, 2014, Pages 285-363

Frustration in biomolecules

Author keywords

[No Author keywords available]

Indexed keywords

BIOPOLYMER;

EID: 84910146695     PISSN: 00335835     EISSN: 14698994     Source Type: Journal    
DOI: 10.1017/S0033583514000092     Document Type: Review
Times cited : (248)

References (243)
  • 2
    • 61849158225 scopus 로고    scopus 로고
    • Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
    • AKSEL, T. & BARRICK, D. (2009). Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models. Methods in Enzymology 455, 95-125. doi: 10.1016/S0076-6879(08)04204-3.
    • (2009) Methods in Enzymology , vol.455 , pp. 95-125
    • Aksel, T.1    Barrick, D.2
  • 3
    • 36149027865 scopus 로고
    • Antiferromagnetism. Theory of superexchange interaction
    • ANDERSON, P.W. (1950). Antiferromagnetism. Theory of superexchange interaction. Physical Review 79, 350-356. doi: 10.1103/PhysRev.79.350. URL: http://link.aps.org/doi/10.1103/PhysRev.79.350.
    • (1950) Physical Review , vol.79 , pp. 350-356
    • Anderson, P.W.1
  • 5
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • ANFINSEN, C. B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 6
    • 84910153577 scopus 로고    scopus 로고
    • Frustration
    • visited on 2013
    • Anonymous (2013). Frustration. Wikipedia, the free encyclopedia. URL: http://en.wikipedia.org/wiki/Frustration (visited on 2013).
    • (2013) Wikipedia, the Free Encyclopedia
    • Anonymous1
  • 8
    • 39149097794 scopus 로고    scopus 로고
    • Folding landscapes of ankyrin repeat proteins: Experiments meet theory
    • BARRICK, D., FERREIRO, D.U. & KOMIVES, E.A. (2008). Folding landscapes of ankyrin repeat proteins: experiments meet theory. Currunet Opinion in Structural Biology 18, 27-34. doi: 10.1016/j.sbi.2007.12.004.
    • (2008) Currunet Opinion in Structural Biology , vol.18 , pp. 27-34
    • Barrick, D.1    Ferreiro, D.U.2    Komives, E.A.3
  • 9
    • 0031029551 scopus 로고    scopus 로고
    • Protein design: The choice of de novo sequences
    • BEASLEY, J.R. & HECHT, M. (1997). Protein design: the choice of de novo sequences. Journal of Biological Chemistry 272, 2031-2034.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 2031-2034
    • Beasley, J.R.1    Hecht, M.2
  • 11
    • 84857033265 scopus 로고    scopus 로고
    • 'Atomistic molecular simulations of protein folding
    • BEST, R. B. (2012). 'Atomistic molecular simulations of protein folding. Currunet Opinion in Structural Biology 22 (1), 52-61. doi: 10.1016/j.sbi.2011.12.001.
    • (2012) Currunet Opinion in Structural Biology , vol.22 , Issue.1 , pp. 52-61
    • Best, R.B.1
  • 13
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • BINZ, H. K., STUMPP, M. T., FORRER, P., AMSTUTZ, P. & PLÜCKTHUN, A. (2003). Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. Journal of Molecular Biology 332, 489-503.
    • (2003) Journal of Molecular Biology , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, P.4    Plückthun, A.5
  • 14
    • 84870835154 scopus 로고    scopus 로고
    • Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy
    • BORGIA, A., WENSLEY, B. G., SORANNO, A., NETTELS, D., BORGIA, M. B., HOFFMANN, A., PFEIL, S. H., LIPMAN, E. A., CLARKE, J. & SCHULER, B. (2012). Localizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy. Nature Communications 3, 1195. doi: 10.1038/ncomms2204.
    • (2012) Nature Communications , vol.3 , pp. 1195
    • Borgia, A.1    Wensley, B.G.2    Soranno, A.3    Nettels, D.4    Borgia, M.B.5    Hoffmann, A.6    Pfeil, S.H.7    Lipman, E.A.8    Clarke, J.9    Schuler, B.10
  • 15
    • 33749054028 scopus 로고    scopus 로고
    • De novo proteins from binarypatterned combinatorial libraries
    • BRADLEY, L. H., THUMFORT, P.P. & HECHT, M. H (2006). De novo proteins from binarypatterned combinatorial libraries. Methods in Molecular Biology 340, 53-69. doi: 10.1385/1-59745-116-9:53.
    • (2006) Methods in Molecular Biology , vol.340 , pp. 53-69
    • Bradley, L.H.1    Thumfort, P.P.2    Hecht, M.H.3
  • 16
    • 0029037739 scopus 로고
    • Protein molecules as computational elements in living cells
    • BRAY, D. (1995). Protein molecules as computational elements in living cells. Nature 376, 307-312. doi: 10.1038/376307a0.
    • (1995) Nature , vol.376 , pp. 307-312
    • Bray, D.1
  • 18
    • 0030983386 scopus 로고    scopus 로고
    • Population statistics of protein structures: Lessons from structural classifications
    • BRENNER, S. E., CHOTHIA, C. & HUBBARD, T. J. (1997). Population statistics of protein structures: lessons from structural classifications. Currunet Opinion in Structural Biology 7, 369-376.
    • (1997) Currunet Opinion in Structural Biology , vol.7 , pp. 369-376
    • Brenner, S.E.1    Chothia, C.2    Hubbard, T.J.3
  • 20
    • 66049146918 scopus 로고    scopus 로고
    • 15N NMR relaxation data reveal significant chemical exchange broadening in the á-domain of human α-lactalbumin
    • BRUYLANTS, G. & REDFIELD, C. (2009). 15N NMR relaxation data reveal significant chemical exchange broadening in the á-domain of human α-lactalbumin. Biochemistry 48, 4031-4039.
    • (2009) Biochemistry , vol.48 , pp. 4031-4039
    • Bruylants, G.1    Redfield, C.2
  • 21
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • BRYNGELSON, J. D., ONUCHIC, J. N., SOCCI, N.D. & WOLYNES, P. G. (1995). Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 23
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • BULLOUGH, P. A., HUGHSON, F. M., SKEHEL, J.J. & WILEY, D. C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43. doi: 10.1038/371037a0.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 24
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • CAPALDI, A. P., KLEANTHOUS, C. & RADFORD, S. E. (2002). Im7 folding mechanism: misfolding on a path to the native state. Nature Structural Biology 9, 209-216. doi: 10.1038/nsb757.
    • (2002) Nature Structural Biology , vol.9 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 26
    • 79955438312 scopus 로고    scopus 로고
    • Diverse pathways of oxidative folding of disulfide proteins: Underlying causes and folding models
    • CHANG, J-Y. (2011). Diverse pathways of oxidative folding of disulfide proteins: underlying causes and folding models. Biochemistry 50, 3414-3431. doi: 10.1021/bi200131j.
    • (2011) Biochemistry , vol.50 , pp. 3414-3431
    • Chang, J.-Y.1
  • 27
    • 84888333782 scopus 로고    scopus 로고
    • 50 Years of allosteric interactions: The twists and turns of the models
    • CHANGEUX, J-P (2013). 50 years of allosteric interactions: the twists and turns of the models. Nature Reviews Molecular Cell Biology. doi: 10.1038/nrm3695.
    • (2013) Nature Reviews Molecular Cell Biology
    • Changeux, J.-P.1
  • 28
    • 0011747222 scopus 로고
    • Structure and properties of metallic glasses
    • CHAUDHARI, P. & TURNBULL, D. (1978). Structure and properties of metallic glasses. Science 199, 11-21.
    • (1978) Science , vol.199 , pp. 11-21
    • Chaudhari, P.1    Turnbull, D.2
  • 29
    • 3142782241 scopus 로고    scopus 로고
    • Quantifying the roughness on the free energy landscape: Entropic bottlenecks and protein folding rates
    • CHAVEZ, L. L., ONUCHIC, J.N. & CLEMENTI, C. (2004). Quantifying the roughness on the free energy landscape: entropic bottlenecks and protein folding rates. Journal of the American Chemical Society 126, 8426-8432. doi: 10.1021/ja049510+.
    • (2004) Journal of the American Chemical Society , vol.126 , pp. 8426-8432
    • Chavez, L.L.1    Onuchic, J.N.2    Clementi, C.3
  • 32
    • 0036968441 scopus 로고    scopus 로고
    • NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability
    • CIERPICKI, T. & OTLEWSKI, J. (2002). NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability. Journal of Molecular Biology 321, 647-658.
    • (2002) Journal of Molecular Biology , vol.321 , pp. 647-658
    • Cierpicki, T.1    Otlewski, J.2
  • 33
    • 0028982611 scopus 로고
    • Sequence 'minimization': Exploring the sequence landscape with simplified sequences
    • CLARKE, N. D. (1995). Sequence 'minimization': exploring the sequence landscape with simplified sequences. Current Opinion in Biotechnology 6, 467-472.
    • (1995) Current Opinion in Biotechnology , vol.6 , pp. 467-472
    • Clarke, N.D.1
  • 34
    • 39149100599 scopus 로고    scopus 로고
    • Coarse-grained models of protein folding: Toy models or predictive tools?
    • CLEMENTI, C. (2008). Coarse-grained models of protein folding: toy models or predictive tools? Currunet Opinion in Structural Biology 18, 10-15. doi: 10.1016/j.sbi.2007.10.005.
    • (2008) Currunet Opinion in Structural Biology , vol.18 , pp. 10-15
    • Clementi, C.1
  • 35
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and 'en-route' intermediates for protein folding? An investigation for small globular proteins
    • CLEMENTI, C., NYMEYER, H. & ONUCHIC, J. N. (2000). Topological and energetic factors: what determines the structural details of the transition state ensemble and 'en-route' intermediates for protein folding? An investigation for small globular proteins. Journal of Molecular Biology 298, 937-953. doi: 10.1006/jmbi.2000.3693.
    • (2000) Journal of Molecular Biology , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3
  • 36
    • 3042677501 scopus 로고    scopus 로고
    • The effects of non-native interactions on protein folding rates: Theory and simulation
    • CLEMENTI, C. & PLOTKIN, S. S. (2004). The effects of non-native interactions on protein folding rates: theory and simulation. Protein Science 13, 1750-1766. doi: 10.1110/ps.03580104.
    • (2004) Protein Science , vol.13 , pp. 1750-1766
    • Clementi, C.1    Plotkin, S.S.2
  • 39
    • 0021659707 scopus 로고
    • Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor
    • CREIGHTON, T.E. & GOLDENBERG, D. P. (1984). Kinetic role of a meta-stable native-like two-disulphide species in the folding transition of bovine pancreatic trypsin inhibitor. Journal of Molecular Biology 179, 497-526.
    • (1984) Journal of Molecular Biology , vol.179 , pp. 497-526
    • Creighton, T.E.1    Goldenberg, D.P.2
  • 40
    • 0015212088 scopus 로고
    • General model for the chromosomes of higher organisms
    • CRICK, F. (1971). General model for the chromosomes of higher organisms. Nature 234, 25-27.
    • (1971) Nature , vol.234 , pp. 25-27
    • Crick, F.1
  • 41
    • 84864213700 scopus 로고    scopus 로고
    • AWSEM-MD: Protein structure prediction using coarse-grained physical potentials and bioinformatically based local structure biasing
    • DAVTYAN, A., SCHAFER, N. P., ZHENG, W., CLEMENTI, C., WOLYNES, P.G. & PAPOIAN, G. A. (2012). AWSEM-MD: protein structure prediction using coarse-grained physical potentials and bioinformatically based local structure biasing. Journal of Physical Chemistry B 116, 8494-8503. doi: 10.1021/jp212541y.
    • (2012) Journal of Physical Chemistry B , vol.116 , pp. 8494-8503
    • Davtyan, A.1    Schafer, N.P.2    Zheng, W.3    Clementi, C.4    Wolynes, P.G.5    Papoian, G.A.6
  • 42
    • 4243861085 scopus 로고
    • Random-energy model: An exactly solvable model of disordered systems
    • DERRIDA, B. (1981). Random-energy model: an exactly solvable model of disordered systems. Physical Review B 2, 2613.
    • (1981) Physical Review B , vol.2 , pp. 2613
    • Derrida, B.1
  • 43
    • 80053588204 scopus 로고    scopus 로고
    • 'The energy landscape analysis of cancer mutations in protein kinases
    • DIXIT, A. & VERKHIVKER, G.M. (2011). 'The energy landscape analysis of cancer mutations in protein kinases. PLoS ONE 6, e26071. doi: 10.1371/journal.pone.0026071.
    • (2011) PLoS ONE , vol.6 , pp. e26071
    • Dixit, A.1    Verkhivker, G.M.2
  • 46
  • 47
    • 0001742061 scopus 로고
    • Activation-energy landscape for metastable RNA folding
    • FERNÁNDEZ, A. & SHAKHNOVICH, E. I. (1990). Activation-energy landscape for metastable RNA folding. Physical Review A 42, 3657-3659.
    • (1990) Physical Review A , vol.42 , pp. 3657-3659
    • Fernández, A.1    Shakhnovich, E.I.2
  • 51
    • 77749298990 scopus 로고    scopus 로고
    • Molecular mechanisms of system control of NF-kappaB signaling by IkappaBalpha
    • FERREIRO, D.U. & KOMIVES, E. A. (2010). Molecular mechanisms of system control of NF-kappaB signaling by IkappaBalpha. Biochemistry 49, 1560-1567. doi: 10.1021/bi901948j.
    • (2010) Biochemistry , vol.49 , pp. 1560-1567
    • Ferreiro, D.U.1    Komives, E.A.2
  • 53
    • 44949165528 scopus 로고    scopus 로고
    • The energy landscapes of repeat-containing proteins: Topology, cooperativity, and the folding funnels of one-dimensional architectures
    • FERREIRO, D. U., WALCZAK, A. M., KOMIVES, E.A. & WOLYNES, P. G. (2008b). The energy landscapes of repeat-containing proteins: topology, cooperativity, and the folding funnels of one-dimensional architectures. PLoS Computational Biology 4, e1000070. doi: 10.1371/journal.pcbi.1000070.
    • (2008) PLoS Computational Biology , vol.4 , pp. e1000070
    • Ferreiro, D.U.1    Walczak, A.M.2    Komives, E.A.3    Wolynes, P.G.4
  • 55
    • 0026511656 scopus 로고
    • The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding
    • FERSHT, A. R., MATOUSCHEK, A. & SERRANO, L. (1992). The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding. Journal of Molecular Biology 224, 771-782.
    • (1992) Journal of Molecular Biology , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 57
    • 84892919674 scopus 로고    scopus 로고
    • Conformational dynamics is more important than helical propensity for the folding of the all alpha-helical protein IM7
    • FIGUEIREDO, A. M., WHITTAKER, S. B.-M., KNOWLING, S. E., RADFORD, S.E. & MOORE, G. R. (2013). Conformational dynamics is more important than helical propensity for the folding of the all alpha-helical protein IM7. Protein Science doi: 10.1002/pro.2372.
    • (2013) Protein Science
    • Figueiredo, A.M.1    Whittaker, S.B.-M.2    Knowling, S.E.3    Radford, S.E.4    Moore, G.R.5
  • 59
    • 0023079867 scopus 로고
    • Function and dynamics of myoglobin
    • FRAUENFELDER, H. (1987). Function and dynamics of myoglobin. Annals of the New York Academy of Sciences 504, 151-167. ISSN: 1749-6632. doi: 10.1111/J.1749-6632.1987.tb48730.x.
    • (1987) Annals of the New York Academy of Sciences , vol.504 , pp. 151-167
    • Frauenfelder, H.1
  • 62
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • FRAUENFELDER, H., SLIGAR, S.G. & WOLYNES, P. G. (1991). The energy landscapes and motions of proteins. Science 254, 1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 63
    • 0021796467 scopus 로고
    • Rate theories and puzzles of hemeprotein kinetics
    • FRAUENFELDER, H. & WOLYNES, P. G. (1985). Rate theories and puzzles of hemeprotein kinetics. Science 299, 337-345.
    • (1985) Science , vol.299 , pp. 337-345
    • Frauenfelder, H.1    Wolynes, P.G.2
  • 64
    • 0001683768 scopus 로고
    • Toward protein tertiary structure recognition by means of associative memory Hamiltonians
    • FRIEDRICHS, M.S. & WOLYNES, P. G. (1989). Toward protein tertiary structure recognition by means of associative memory Hamiltonians. Science 246, 371-373.
    • (1989) Science , vol.246 , pp. 371-373
    • Friedrichs, M.S.1    Wolynes, P.G.2
  • 65
    • 62049084565 scopus 로고    scopus 로고
    • The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints
    • FRIEL, C. T., SMITH, D. A., VENDRUSCOLO, M., GSPONER, J. & RADFORD, S. E. (2009). The mechanism of folding of Im7 reveals competition between functional and kinetic evolutionary constraints. Nature Structural & Molecular Biology 16, 318-324. doi: 10.1038/nsmb.1562.
    • (2009) Nature Structural & Molecular Biology , vol.16 , pp. 318-324
    • Friel, C.T.1    Smith, D.A.2    Vendruscolo, M.3    Gsponer, J.4    Radford, S.E.5
  • 69
    • 0033517740 scopus 로고    scopus 로고
    • Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxyterminal domain of T4 lysozyme is a rate-limiting step in folding
    • GASSNER, N. C., BAASE, W. A., LINDSTROM, J. D., LU, J., DAHLQUIST, F.W., & MATTHEWS, B.W. (1999). Methionine and alanine substitutions show that the formation of wild-type-like structure in the carboxyterminal domain of T4 lysozyme is a rate-limiting step in folding. Biochemistry 38, 14451-14460.
    • (1999) Biochemistry , vol.38 , pp. 14451-14460
    • Gassner, N.C.1    Baase, W.A.2    Lindstrom, J.D.3    Lu, J.4    Dahlquist, F.W.5    Matthews, B.W.6
  • 71
    • 0023468862 scopus 로고
    • The exon theory of genes
    • New York, NY: Cold Spring Harbor Laboratory Press
    • GILBERT, W. (1987). The exon theory of genes. In Cold Spring Harbor Symposia on Quantitative Biology, vol. 52. New York, NY: Cold Spring Harbor Laboratory Press, pp. 901-905.
    • (1987) Cold Spring Harbor Symposia on Quantitative Biology , vol.52 , pp. 901-905
    • Gilbert, W.1
  • 72
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • GO, N. (1983). Theoretical studies of protein folding. Annual Review of Biophysics and Bioengineering 12, 183-210. doi: 10.1146/annurev.bb.12.060183.001151.
    • (1983) Annual Review of Biophysics and Bioengineering , vol.12 , pp. 183-210
    • Go, N.1
  • 75
    • 33645030244 scopus 로고    scopus 로고
    • Topological frustration and the folding of interleukin-1 beta
    • GOSAVI, S., CHAVEZ, L. L., JENNINGS, P.A. & ONUCHIC, J. N. (2006). Topological frustration and the folding of interleukin-1 beta. Journal of Molecular Biology 357, 986-996. doi: 10.1016/j.jmb.2005.11.074.
    • (2006) Journal of Molecular Biology , vol.357 , pp. 986-996
    • Gosavi, S.1    Chavez, L.L.2    Jennings, P.A.3    Onuchic, J.N.4
  • 79
    • 84867025667 scopus 로고    scopus 로고
    • Modulation of folding kinetics of repeat proteins: Interplay between intra- and interdomain interactions
    • HAGAI, T., AZIA, A., TRIZAC, E. & LEVY, Y. (2012). Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions. Biophysical Journal 103, 1555-1565. doi: 10.1016/j.bpj.2012.08.018.
    • (2012) Biophysical Journal , vol.103 , pp. 1555-1565
    • Hagai, T.1    Azia, A.2    Trizac, E.3    Levy, Y.4
  • 81
    • 69749119200 scopus 로고    scopus 로고
    • The spectrum of biomolecular states and motions
    • HEGLER, J. A., WEINKAM, P. & WOLYNES, P. G. (2008). The spectrum of biomolecular states and motions. HFSP Journal 2, 307-313.
    • (2008) HFSP Journal , vol.2 , pp. 307-313
    • Hegler, J.A.1    Weinkam, P.2    Wolynes, P.G.3
  • 86
    • 47249140371 scopus 로고    scopus 로고
    • Design of an active ultrastable single-chain insulin analog: Synthesis, structure, and therapeutic implications
    • HUA, Q.-X., NAKAGAWA, S. H., JIA, W., HUANG, K., PHILLIPS, N. B., HU, S.-Q. & WEISS, M. A. (2008). Design of an active ultrastable single-chain insulin analog: synthesis, structure, and therapeutic implications. Journal of Biological Chemistry 283, 14703-14716. doi: 10.1074/jbc.M800313200.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 14703-14716
    • Hua, Q.-X.1    Nakagawa, S.H.2    Jia, W.3    Huang, K.4    Phillips, N.B.5    Hu, S.-Q.6    Weiss, M.A.7
  • 87
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • HUNTINGTON, J. A., READ, R. J. & CARRELL, R.W. (2000). Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926. doi: 10.1038/35038119.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 88
    • 0033837714 scopus 로고    scopus 로고
    • Bypassing the kinetic trap of serpin protein folding by loop extension
    • IM, H., AHN, H.Y. & YU, M. H. (2000). Bypassing the kinetic trap of serpin protein folding by loop extension. Protein Science 9, 1497-1502. doi: 10.1110/ps.9.8.1497.
    • (2000) Protein Science , vol.9 , pp. 1497-1502
    • Im, H.1    Ahn, H.Y.2    Yu, M.H.3
  • 89
    • 84866786956 scopus 로고    scopus 로고
    • From artificial antibodies to nanosprings: The biophysical properties of repeat proteins
    • ITZHAKI, L.S. & LOWE, A. R. (2012). From artificial antibodies to nanosprings: the biophysical properties of repeat proteins. Advances in Experimental Medicine and Biology 747, 153-166. doi: 10.1007/978-1-4614-3229-6-10.
    • (2012) Advances in Experimental Medicine and Biology , vol.747 , pp. 153-166
    • Itzhaki, L.S.1    Lowe, A.R.2
  • 90
    • 0036400715 scopus 로고    scopus 로고
    • Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance
    • JANE DYSON, H. & WRIGHT, P. E. (2002). Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance. Advances in Protein Chemistry 62, 311-340.
    • (2002) Advances in Protein Chemistry , vol.62 , pp. 311-340
    • Jane Dyson, H.1    Wright, P.E.2
  • 91
    • 70350465130 scopus 로고    scopus 로고
    • Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins
    • JAVADI, Y. & MAIN, E. R. G. (2009). Exploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins. Proceedings of the National Academy of Sciences of the United States of America 106, 17383-17388. doi: 10.1073/pnas.0907455106.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , pp. 17383-17388
    • Javadi, Y.1    Main, E.R.G.2
  • 92
    • 84864449930 scopus 로고    scopus 로고
    • Protein frustratometer: A tool to localize energetic frustration in protein molecules
    • JENIK, M., PARRA, R. G., RADUSKY, L. G., TRUCHANSKI, A., WOLYNES, P.G. & FERREIRO, D. U. (2012). Protein frustratometer: a tool to localize energetic frustration in protein molecules. Nucleic Acids Research 40(Web Server issue), W348-W351. doi: 10.1093/nar/gks447.
    • (2012) Nucleic Acids Research , vol.40 , Issue.WEB SERVER ISSUE , pp. W348-W351
    • Jenik, M.1    Parra, R.G.2    Radusky, L.G.3    Truchanski, A.4    Wolynes, P.G.5    Ferreiro, D.U.6
  • 93
    • 0038242197 scopus 로고    scopus 로고
    • De novo design of foldable proteins with smooth folding funnel: Automated negative design and experimental verification
    • JIN, W., KAMBARA, O., SASAKAWA, H., TAMURA, A. & TAKADA, S. (2003). De novo design of foldable proteins with smooth folding funnel: automated negative design and experimental verification. Structure 11, 581-590.
    • (2003) Structure , vol.11 , pp. 581-590
    • Jin, W.1    Kambara, O.2    Sasakawa, H.3    Tamura, A.4    Takada, S.5
  • 94
    • 84865174088 scopus 로고    scopus 로고
    • Tandem repeats in proteins: From sequence to structure
    • KAJAVA, A. V. (2012). Tandem repeats in proteins: from sequence to structure. Journal of Structural Biology 179, 279-288. doi: 10.1016/j.jsb.2011.08.009.
    • (2012) Journal of Structural Biology , vol.179 , pp. 279-288
    • Kajava, A.V.1
  • 95
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • KAMTEKAR, S., SCHIFFER, J. M., XIONG, H., BABIK, J.M. & 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
  • 96
    • 0020698476 scopus 로고
    • Dynamics of proteins: Elements and function
    • KARPLUS, M. & MCCAMMON, J. A. (1983). Dynamics of proteins: elements and function. Annual Review in Biochemistry 52, 263-300. doi: 10.1146/annurev.bi.52.070183.001403.
    • (1983) Annual Review in Biochemistry , vol.52 , pp. 263-300
    • Karplus, M.1    McCammon, J.A.2
  • 97
    • 34548185862 scopus 로고    scopus 로고
    • Thermodynamic properties of BPTI variants with highly simplified amino acid sequences
    • KATO, A., YAMADA, M., NAKAMURA, S., KIDOKORO, S.-I. & KURODA, Y. (2007). Thermodynamic properties of BPTI variants with highly simplified amino acid sequences. Journal of Molecular Biology 372, 737-746. doi: 10.1016/j.jmb.2007.06.066.
    • (2007) Journal of Molecular Biology , vol.372 , pp. 737-746
    • Kato, A.1    Yamada, M.2    Nakamura, S.3    Kidokoro, S.-I.4    Kuroda, Y.5
  • 99
    • 0043027950 scopus 로고
    • Forces responsible for maintaining the native configurations of proteins
    • KAUZMANN, W. (1959). Forces responsible for maintaining the native configurations of proteins. Advances in Protein Chemistry 14, 33-35.
    • (1959) Advances in Protein Chemistry , vol.14 , pp. 33-35
    • Kauzmann, W.1
  • 100
    • 0035810165 scopus 로고    scopus 로고
    • Functional proteins from a random-sequence library
    • KEEFE, A.D. & SZOSTAK, J.W. (2001). Functional proteins from a random-sequence library. Nature 410, 715-718. doi: 10.1038/35070613.
    • (2001) Nature , vol.410 , pp. 715-718
    • Keefe, A.D.1    Szostak, J.W.2
  • 101
    • 0036295960 scopus 로고    scopus 로고
    • Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains
    • KLIMOV, D.K. & THIRUMALAI, D. (2002). Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains. Journal of Molecular Biology 317, 721-737. doi: 10.1006/jmbi.2002.5453.
    • (2002) Journal of Molecular Biology , vol.317 , pp. 721-737
    • Klimov, D.K.1    Thirumalai, D.2
  • 102
    • 0029895539 scopus 로고    scopus 로고
    • Self-consistently optimized statistical mechanical energy functions for sequence structure alignment
    • KORETKE, K. K., LUTHEY-SCHULTEN, Z. & WOLYNES, P.G. (1996). Self-consistently optimized statistical mechanical energy functions for sequence structure alignment. Protein Science 5, 1043-1059.
    • (1996) Protein Science , vol.5 , pp. 1043-1059
    • Koretke, K.K.1    Luthey-Schulten, Z.2    Wolynes, P.G.3
  • 103
    • 78349313323 scopus 로고    scopus 로고
    • Structural determinants for improved stability of designed ankyrin repeat proteins with a redesigned C-capping module
    • KRAMER, M. A., WETZEL, S. K., PLÜCKTHUN, A., MITTL, P.R.E. & GRÜTTER, M. G. (2010). Structural determinants for improved stability of designed ankyrin repeat proteins with a redesigned C-capping module. Journal of Molecular Biology 404, 381-391. doi: 10.1016/j.jmb.2010.09.023.
    • (2010) Journal of Molecular Biology , vol.404 , pp. 381-391
    • Kramer, M.A.1    Wetzel, S.K.2    Plückthun, A.3    Mittl, P.R.E.4    Grütter, M.G.5
  • 104
    • 0346168895 scopus 로고
    • Syncategoremata, exponibilia, sophismata
    • (eds. N. KRETZMANN, A. KENNY & J. PINBORG), Cambridge: Cambridge University Press
    • KRETZMANN, N. (1982). Syncategoremata, exponibilia, sophismata. In The Cambridge History of Later Medieval Philosophy (eds. N. KRETZMANN, A. KENNY & J. PINBORG), pp. 211-245. Cambridge: Cambridge University Press.
    • (1982) The Cambridge History of Later Medieval Philosophy , pp. 211-245
    • Kretzmann, N.1
  • 105
    • 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. & BAKER, D. (2003). Design of a novel globular protein fold with atomic-level accuracy. Science 302, 1364-1368. doi: 10.1126/Science.1089427.
    • (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
  • 106
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • KURIYAN, J. & EISENBERG, D. (2007). The origin of protein interactions and allostery in colocalization. Nature 450, 983-990. doi: 10.1038/nature06524.
    • (2007) Nature , vol.450 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 107
    • 0034607555 scopus 로고    scopus 로고
    • Folding of bovine pancreatic trypsin inhibitor (BPTI) variants in which almost half the residues are alanine
    • KURODA, Y. & KIM, P. S. (2000). Folding of bovine pancreatic trypsin inhibitor (BPTI) variants in which almost half the residues are alanine. Journal of Molecular Biology 298, 493-501. doi: 10.1006/jmbi.2000.3622.
    • (2000) Journal of Molecular Biology , vol.298 , pp. 493-501
    • Kuroda, Y.1    Kim, P.S.2
  • 109
    • 0000288714 scopus 로고
    • Parameters for the description of transition states
    • LEFFLER, J. E. (1953). Parameters for the description of transition states. Science 117, 340-341. doi: 10.1126/science.117.3039.340.
    • (1953) Science , vol.117 , pp. 340-341
    • Leffler, J.E.1
  • 110
    • 0002006297 scopus 로고
    • Are there pathways for protein folding
    • LEVINTHAL, C. (1968). Are there pathways for protein folding. Journal de Chimie Physique 65, 44-45.
    • (1968) Journal de Chimie Physique , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 112
    • 33846625611 scopus 로고    scopus 로고
    • Fly-casting in protein-DNA binding: Frustration between protein folding and electrostatics facilitates target recognition
    • LEVY, Y., ONUCHIC, J.N. & WOLYNES, P. G. (2007). Fly-casting in protein-DNA binding: frustration between protein folding and electrostatics facilitates target recognition. Journal of the American Chemical Society 129, 738-739. doi: 10.1021/ja065531n.
    • (2007) Journal of the American Chemical Society , vol.129 , pp. 738-739
    • Levy, Y.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 114
    • 0015951617 scopus 로고
    • The existence of persistent states in the brain
    • LITTLE, W. A. (1974). The existence of persistent states in the brain. Mathematical Biosciences 19, 101-120.
    • (1974) Mathematical Biosciences , vol.19 , pp. 101-120
    • Little, W.A.1
  • 115
    • 0034614649 scopus 로고    scopus 로고
    • The introduction of strain and its effects on the structure and stability of T4 lysozyme
    • LIU, R., BAASE, W.A. & MATTHEWS, B.W. (2000). The introduction of strain and its effects on the structure and stability of T4 lysozyme. Journal of Molecular Biology 295, 127-145. doi: 10.1006/jmbi.1999.3300.
    • (2000) Journal of Molecular Biology , vol.295 , pp. 127-145
    • Liu, R.1    Baase, W.A.2    Matthews, B.W.3
  • 118
    • 0001143109 scopus 로고
    • Helix-coil, liquid crystal, and spin glass transitions of a collapsed heteropolymer
    • LUTHEY-SCHULTEN, Z., RAMIREZ, B.E. & WOLYNES, P.G. (1995). Helix-coil, liquid crystal, and spin glass transitions of a collapsed heteropolymer. Journal of Physical Chemistry 99, 2177-2185.
    • (1995) Journal of Physical Chemistry , vol.99 , pp. 2177-2185
    • Luthey-Schulten, Z.1    Ramirez, B.E.2    Wolynes, P.G.3
  • 121
    • 84886671899 scopus 로고    scopus 로고
    • Weak frustration regulates sliding and binding kinetics on rugged protein- DNA landscapes
    • MARCOVITZ, A. & LEVY, Y. (2013). Weak frustration regulates sliding and binding kinetics on rugged protein- DNA landscapes. Journal of Physical Chemistry B 112, 13005-13014. doi: 10.1021/jp402296d.
    • (2013) Journal of Physical Chemistry B , vol.112 , pp. 13005-13014
    • Marcovitz, A.1    Levy, Y.2
  • 122
    • 79959409852 scopus 로고    scopus 로고
    • The shape-shifting quasispecies of RNA: One sequence, many functional folds
    • MAREK, M. S., JOHNSON-BUCK, A. & WALTER, N. G. (2011). The shape-shifting quasispecies of RNA: one sequence, many functional folds. Physical Chemistry Chemical Physics 13, 11524-11537. doi: 10.1030/c1cp20576e.
    • (2011) Physical Chemistry Chemical Physics , vol.13 , pp. 11524-11537
    • Marek, M.S.1    Johnson-Buck, A.2    Walter, N.G.3
  • 123
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • MATOUSCHEK, A., KELLIS, J. T. Jr., SERRANO, L. & FERSHT, A. R. (1989). Mapping the transition state and pathway of protein folding by protein engineering. Nature 340, 122-126. doi: 10.1038/340122a0.
    • (1989) Nature , vol.340 , pp. 122-126
    • Matouschek, A.1    Kellis, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 124
    • 0023358977 scopus 로고
    • Mutant sequences as probes of protein folding mechanisms
    • MATTHEWS, C.R. & HURLE, M. R. (1987). Mutant sequences as probes of protein folding mechanisms. Bioessays 6, 254-257. doi: 10.1002/bies.950060603.
    • (1987) Bioessays , vol.6 , pp. 254-257
    • Matthews, C.R.1    Hurle, M.R.2
  • 125
    • 0032821685 scopus 로고    scopus 로고
    • Towards more meaningful hierarchical classification of amino acid scoring matrices
    • MAY, A. C. (1999). Towards more meaningful hierarchical classification of amino acid scoring matrices. Protein Engineering 12, 707-712.
    • (1999) Protein Engineering , vol.12 , pp. 707-712
    • May, A.C.1
  • 126
    • 0026723477 scopus 로고
    • Effect of active site residues in barnase on activity and stability
    • MEIERING, E. M., SERRANO, L. & FERSHT, A. R. (1992). Effect of active site residues in barnase on activity and stability. Journal of Molecular Biology 225, 585-589.
    • (1992) Journal of Molecular Biology , vol.225 , pp. 585-589
    • Meiering, E.M.1    Serrano, L.2    Fersht, A.R.3
  • 127
    • 0000713579 scopus 로고    scopus 로고
    • Designability, thermodynamic stability, and dynamics in protein folding: A lattice model study
    • MÉLIN, R., LI, H., WINGREEN, N.S. & TANG, C. (1999). Designability, thermodynamic stability, and dynamics in protein folding: a lattice model study. Journal of Chemical Physics 110, 1252.
    • (1999) Journal of Chemical Physics , vol.110 , pp. 1252
    • Mélin, R.1    Li, H.2    Wingreen, N.S.3    Tang, C.4
  • 129
    • 70149115237 scopus 로고    scopus 로고
    • Constraint satisfaction problems and neural networks: A statistical physics perspective
    • MÉZARD, M. & MORA, T. (2009). Constraint satisfaction problems and neural networks: a statistical physics perspective. Journal of Physiology - Paris 103, 107-113.
    • (2009) Journal of Physiology - Paris , vol.103 , pp. 107-113
    • Mézard, M.1    Mora, T.2
  • 131
    • 0033536221 scopus 로고    scopus 로고
    • Determining computational complexity from characteristic 'phase transitions'
    • MONASSON, R., ZECCHINA, R., KIRKPATRICK, S., SELMAN, B. & TROYANSKY, L. (1999). Determining computational complexity from characteristic 'phase transitions'. Nature 400, 133-137.
    • (1999) Nature , vol.400 , pp. 133-137
    • Monasson, R.1    Zecchina, R.2    Kirkpatrick, S.3    Selman, B.4    Troyansky, L.5
  • 134
    • 0030627747 scopus 로고    scopus 로고
    • Speeding up protein folding: Mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude
    • MUNSON, M., ANDERSON, K.S. & REGAN, L. (1997). Speeding up protein folding: mutations that increase the rate at which Rop folds and unfolds by over four orders of magnitude. Folding and Designing 2, 77-87.
    • (1997) Folding and Designing , vol.2 , pp. 77-87
    • Munson, M.1    Anderson, K.S.2    Regan, L.3
  • 135
    • 0001338954 scopus 로고    scopus 로고
    • Simplified amino acid alphabets for protein fold recognition and implications for folding
    • MURPHY, L. R., WALLQVIST, A. & LEVY, R.M. (2000). Simplified amino acid alphabets for protein fold recognition and implications for folding. Protein Engineering 13, 149-152.
    • (2000) Protein Engineering , vol.13 , pp. 149-152
    • Murphy, L.R.1    Wallqvist, A.2    Levy, R.M.3
  • 137
    • 39749156038 scopus 로고
    • Magnetism and the local molecular field
    • (ed. G. EKSPONG), Amsterdam: Elsevier
    • NÉEL, L. (1970). Magnetism and the local molecular field. In Nobel Lectures, vol. Physics 1963-1970 (ed. G. EKSPONG), pp. 318-341. Amsterdam: Elsevier.
    • (1970) Nobel Lectures, Vol. Physics 1963-1970 , pp. 318-341
    • Néel, L.1
  • 138
    • 84864212951 scopus 로고    scopus 로고
    • The shadow map: A general contact definition for capturing the dynamics of biomolecular folding and function
    • NOEL, J. K., WHITFORD, P.C. & ONUCHIC, J. N. (2012). The shadow map: a general contact definition for capturing the dynamics of biomolecular folding and function. Journal of Physical Chemistry B 116, 8692-8702. doi: 10.1021/jp300852d.
    • (2012) Journal of Physical Chemistry B , vol.116 , pp. 8692-8702
    • Noel, J.K.1    Whitford, P.C.2    Onuchic, J.N.3
  • 139
    • 77954276842 scopus 로고    scopus 로고
    • SMOG@ctbp: Simplified deployment of structure-based models in GROMACS
    • NOEL, J. K., WHITFORD, P. C., SANBONMATSU, K.Y. & ONUCHIC, J. N. (2010). SMOG@ctbp: simplified deployment of structure-based models in GROMACS. Nucleic Acids Research 38(Web Server issue), W657-W661. doi: 10.1093/nar/gkq498.
    • (2010) Nucleic Acids Research , vol.38 , Issue.WEB SERVER ISSUE , pp. W657-W661
    • Noel, J.K.1    Whitford, P.C.2    Sanbonmatsu, K.Y.3    Onuchic, J.N.4
  • 140
    • 77952246173 scopus 로고    scopus 로고
    • The protein-DNA Interface database
    • NORAMBUENA, T. & MELO, F. (2010). The protein-DNA Interface database. BMC Bioinformatics 11, 262. doi: 10.1186/1471-2105-11-262.
    • (2010) BMC Bioinformatics , vol.11 , pp. 262
    • Norambuena, T.1    Melo, F.2
  • 141
    • 84887255391 scopus 로고    scopus 로고
    • Competing interaction in magnets: The root of ordered disorder or only frustration?
    • NORDBLAD, P. (2013). Competing interaction in magnets: the root of ordered disorder or only frustration? Physica Scripta 88, 058301.
    • (2013) Physica Scripta , vol.88 , pp. 058301
    • Nordblad, P.1
  • 142
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • OLIVEBERG, M. & WOLYNES, P. G. (2005). The experimental survey of protein-folding energy landscapes. Quarterly Reviews of Biophysics 38, 245-288.
    • (2005) Quarterly Reviews of Biophysics , vol.38 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 143
    • 33646935697 scopus 로고    scopus 로고
    • Dynamical contributions to enzyme catalysis: Critical tests of a popular hypothesis
    • OLSSON, M. H. M., PARSON, W.W. & WARSHEL, A. (2006). Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis. Chemical Reviews 106, 1737-1756. doi: 10.1021/cr040427e.
    • (2006) Chemical Reviews , vol.106 , pp. 1737-1756
    • Olsson, M.H.M.1    Parson, W.W.2    Warshel, A.3
  • 149
    • 0042868638 scopus 로고    scopus 로고
    • Role of water mediated interactions in protein-protein recognition landscapes
    • PAPOIAN, G. A., ULANDER, J. & WOLYNES, P. G. (2003a). Role of water mediated interactions in protein-protein recognition landscapes. Journal of the American Chemical Society 125, 9170-9178. doi: 10.1021/ja034729u.
    • (2003) Journal of the American Chemical Society , vol.125 , pp. 9170-9178
    • Papoian, G.A.1    Ulander, J.2    Wolynes, P.G.3
  • 150
    • 0037346726 scopus 로고    scopus 로고
    • The physics and bioinformatics of binding and folding-an energy landscape perspective
    • PAPOIAN, G.A. & WOLYNES, P. G. (2003b). The physics and bioinformatics of binding and folding-an energy landscape perspective. Biopolymers 68, 333-349. doi: 10.1002/bip.10286.
    • (2003) Biopolymers , vol.68 , pp. 333-349
    • Papoian, G.A.1    Wolynes, P.G.2
  • 151
    • 84886688567 scopus 로고    scopus 로고
    • Detecting repetitions and periodicities in proteins by tiling the structural space
    • PARRA, R. G., ESPADA, R., SÁNCHEZ, I. E., SIPPL, M. J. & FERREIRO, D. U. (2013). Detecting repetitions and periodicities in proteins by tiling the structural space. Journal of Physical Chemistry B 117, 12887-12897. doi: 10.1021/jp402105j.
    • (2013) Journal of Physical Chemistry B , vol.117 , pp. 12887-12897
    • Parra, R.G.1    Espada, R.2    Sánchez, I.E.3    Sippl, M.J.4    Ferreiro, D.U.5
  • 153
    • 79959720287 scopus 로고    scopus 로고
    • How robust are protein folding simulations with respect to force field parameterization?
    • PIANA, S., LINDORFF-LARSEN, K. & SHAW, D. E. (2011). How robust are protein folding simulations with respect to force field parameterization? Biophysical Journal 100, L47-L49. doi: 10.1016/j.bpj.2011.03.051.
    • (2011) Biophysical Journal , vol.100 , pp. L47-L49
    • Piana, S.1    Lindorff-Larsen, K.2    Shaw, D.E.3
  • 155
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • PLAXCO, K.W., SIMONS, K.T. & BAKER, D. (1998). Contact order, transition state placement and the refolding rates of single domain proteins. Journal of Molecular Biology 277, 985-994. doi: 10.1006/jmbi.1998.1645.
    • (1998) Journal of Molecular Biology , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 156
    • 0036023918 scopus 로고    scopus 로고
    • Understanding protein folding with energy landscape theory. Part I: Basic concepts
    • PLOTKIN, S.S. & ONUCHIC, J. N. (2002). Understanding protein folding with energy landscape theory. Part I: basic concepts. Quarterly Reviews of Biophysics 35, 111-167.
    • (2002) Quarterly Reviews of Biophysics , vol.35 , pp. 111-167
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 157
    • 0030165480 scopus 로고    scopus 로고
    • Correlated energy landscape model for finite, random heteropolymers
    • PLOTKIN, S. S., WANG, J. & WOLYNES, P. G. (1996). Correlated energy landscape model for finite, random heteropolymers. Physical Review E 53, 6271.
    • (1996) Physical Review E , vol.53 , pp. 6271
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 158
    • 0007463680 scopus 로고    scopus 로고
    • Statistical mechanics of a correlated energy landscape model for protein folding funnels
    • PLOTKIN, S. S., WANG, J. & WOLYNES, P. G. (1997). Statistical mechanics of a correlated energy landscape model for protein folding funnels. Journal of Chemical Physics 106, 2932-2948. doi: http://dx.doi.org/10.1063/1.473355.
    • (1997) Journal of Chemical Physics , vol.106 , pp. 2932-2948
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3
  • 159
    • 0345864027 scopus 로고    scopus 로고
    • The Catalytic Site Atlas: A resource of catalytic sites and residues identified in enzymes using structural data
    • PORTER, C. T., BARTLETT, G. J. & THORNTON, J.M. (2004). The Catalytic Site Atlas: a resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Research 32(Database issue), D129-D133. doi: 10.1093/nar/gkh028.
    • (2004) Nucleic Acids Research , vol.32 , Issue.DATABASE ISSUE , pp. D129-D133
    • Porter, C.T.1    Bartlett, G.J.2    Thornton, J.M.3
  • 160
    • 0000227308 scopus 로고    scopus 로고
    • Variational theory for site resolved protein folding free energy surfaces
    • PORTMAN, J. J., TAKADA, S. & WOLYNES, P. G. (1998). Variational theory for site resolved protein folding free energy surfaces. Physical Review Letters 81, 5237.
    • (1998) Physical Review Letters , vol.81 , pp. 5237
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 161
    • 0035868476 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approach
    • PORTMAN, J. J., TAKADA, S. & WOLYNES, P. G. (2001a). Microscopic theory of protein folding rates. I. Fine structure of the free energy profile and folding routes from a variational approach. Journal of Chemical Physics 114, 5237-5240.
    • (2001) Journal of Chemical Physics , vol.114 , pp. 5237-5240
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 162
    • 0035868526 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics
    • PORTMAN, J. J., TAKADA, S. & WOLYNES, P. G. (2001b). Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics. Journal of Chemical Physics 114, 5082.
    • (2001) Journal of Chemical Physics , vol.114 , pp. 5082
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 163
    • 70449555973 scopus 로고    scopus 로고
    • Folding of electrostatically charged beads-on-a-string as an experimental realization of a theoretical model in polymer science
    • RECHES, M., SNYDER, P.W. & WHITESIDES, G.M. (2009). Folding of electrostatically charged beads-on-a-string as an experimental realization of a theoretical model in polymer science. Proceedings of the National Academy of Sciences of the United States of America 106, 17644-17649. doi: 10.1073/pnas.0905533106.
    • (2009) Proceedings of the National Academy of Sciences of the United States of America , vol.106 , pp. 17644-17649
    • Reches, M.1    Snyder, P.W.2    Whitesides, G.M.3
  • 165
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • ROTHEMUND, P.W. K. (2006). Folding DNA to create nanoscale shapes and patterns. Nature 440, 297-302. doi: 10.1038/nature04586.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.K.1
  • 166
    • 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. Journal of Molecular Biology 235, 1614-1636.
    • (1994) Journal of Molecular Biology , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 167
    • 0037225280 scopus 로고    scopus 로고
    • Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding
    • SÁNCHEZ, I.E. & KIEFHABER, T. (2003a). Evidence for sequential barriers and obligatory intermediates in apparent two-state protein folding. Journal of Molecular Biology 325, 367-376.
    • (2003) Journal of Molecular Biology , vol.325 , pp. 367-376
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 168
    • 0037438623 scopus 로고    scopus 로고
    • Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding
    • SÁNCHEZ, I.E. & KIEFHABER, T. (2003b). Non-linear rate-equilibrium free energy relationships and Hammond behavior in protein folding. Biophysical Chemistry 100, 397-407.
    • (2003) Biophysical Chemistry , vol.100 , pp. 397-407
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 170
    • 78650479464 scopus 로고    scopus 로고
    • Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding
    • SÁNCHEZ, I. E., FERREIRO, D.U. & DE PRAT GAY, G. (2011). Mutational analysis of kinetic partitioning in protein folding and protein-DNA binding. Protein Engineering Design and Selection 24, 179-184. doi: 10.1093/protein/gzq064.
    • (2011) Protein Engineering Design and Selection , vol.24 , pp. 179-184
    • Sánchez, I.E.1    Ferreiro, D.U.2    De Prat Gay, G.3
  • 171
    • 1842635571 scopus 로고    scopus 로고
    • Characterization of the folding energy landscapes of computer generated proteins suggests high folding free energy barriers and cooperativity may be consequences of natural selection
    • SCALLEY-KIM, M. & BAKER, D. (2004). Characterization of the folding energy landscapes of computer generated proteins suggests high folding free energy barriers and cooperativity may be consequences of natural selection. Journal of Molecular Biology 338, 573-583. doi: 10.1016/j.jmb.2004.02.055.
    • (2004) Journal of Molecular Biology , vol.338 , pp. 573-583
    • Scalley-Kim, M.1    Baker, D.2
  • 172
    • 84871229676 scopus 로고    scopus 로고
    • Discrete kinetic models from funneled energy landscape simulations
    • SCHAFER, N. P., HOFFMAN, R.M. B., BURGER, A., CRAIG, P. O., KOMIVES, E.A. & WOLYNES, P.G. (2012). Discrete kinetic models from funneled energy landscape simulations. PLoS ONE 7, e50635. doi: 10.1371/journal.pone.0050635.
    • (2012) PLoS ONE , vol.7 , pp. e50635
    • Schafer, N.P.1    Hoffman, R.M.B.2    Burger, A.3    Craig, P.O.4    Komives, E.A.5    Wolynes, P.G.6
  • 173
    • 0014062165 scopus 로고
    • Use of helical wheels to represent the structures of proteins and to identify segments with helical potential
    • SCHIFFER, M. & EDMUNDSON, A. B. (1967). Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophysical Journal 7, 121-135.
    • (1967) Biophysical Journal , vol.7 , pp. 121-135
    • Schiffer, M.1    Edmundson, A.B.2
  • 174
    • 0002450027 scopus 로고    scopus 로고
    • Recent experimental progress in the study of geometrical magnetic frustration
    • SCHIFFER, P. & RAMIREZ, A. P. (1996). Recent experimental progress in the study of geometrical magnetic frustration. Comments on Condensed Matter Physics 18, 21-50.
    • (1996) Comments on Condensed Matter Physics , vol.18 , pp. 21-50
    • Schiffer, P.1    Ramirez, A.P.2
  • 175
    • 0013822867 scopus 로고
    • Dependence of the melting temperature of DNA on salt concentration
    • SCHILDKRAUT, C. & LIFSON, S. (1965). Dependence of the melting temperature of DNA on salt concentration. Biopolymers 3, 195-208. doi: 10.1002/bip.360030207.
    • (1965) Biopolymers , vol.3 , pp. 195-208
    • Schildkraut, C.1    Lifson, S.2
  • 176
    • 84872543206 scopus 로고    scopus 로고
    • A decade of riboswitches
    • SERGANOV, A. & NUDLER, E. (2013). A decade of riboswitches. Cell 152, 17-24. doi: 10.1016/j.cell.2012.12.024.
    • (2013) Cell , vol.152 , pp. 17-24
    • Serganov, A.1    Nudler, E.2
  • 177
    • 36549097257 scopus 로고
    • Enumeration of all compact conformations of copolymers with random sequence of links
    • SHAKHNOVICH, E. & GUTIN, A. (1990). Enumeration of all compact conformations of copolymers with random sequence of links. Journal of Chemical Physics 93, 5967.
    • (1990) Journal of Chemical Physics , vol.93 , pp. 5967
    • Shakhnovich, E.1    Gutin, A.2
  • 178
    • 17844377028 scopus 로고    scopus 로고
    • Scanning malleable transition state ensembles: Comparing theory and experiment for folding protein U1A
    • SHEN, T., HOFMANN, C. P., OLIVEBERG, M. & WOLYNES, P. G. (2005). Scanning malleable transition state ensembles: comparing theory and experiment for folding protein U1A. Biochemistry 44, 6433-6439.
    • (2005) Biochemistry , vol.44 , pp. 6433-6439
    • Shen, T.1    Hofmann, C.P.2    Oliveberg, M.3    Wolynes, P.G.4
  • 180
    • 0033515615 scopus 로고    scopus 로고
    • Exploring structures in protein folding funnels with free energy functionals: The transition state ensemble
    • SHOEMAKER, B. A., WANG, J. & WOLYNES, P. G. (1999). Exploring structures in protein folding funnels with free energy functionals: the transition state ensemble. Journal of Molecular Biology 287, 675-694. doi: 10.1006/jmbi.1999.2613.
    • (1999) Journal of Molecular Biology , vol.287 , pp. 675-694
    • Shoemaker, B.A.1    Wang, J.2    Wolynes, P.G.3
  • 183
    • 84859379149 scopus 로고    scopus 로고
    • Detection of spatial correlations in protein structures and molecular complexes
    • SIPPL, M.J. & WIEDERSTEIN, M. (2012). Detection of spatial correlations in protein structures and molecular complexes. Structure 20, 718-728. doi: 10.1016/j.str.2012.01.024.
    • (2012) Structure , vol.20 , pp. 718-728
    • Sippl, M.J.1    Wiederstein, M.2
  • 184
    • 10044223573 scopus 로고    scopus 로고
    • Kinetics of protein-DNA interaction: Facilitated target location in sequencedependent potential
    • SLUTSKY, M. & MIRNY, L. A. (2004). Kinetics of protein-DNA interaction: facilitated target location in sequencedependent potential. Biophysical Journal 87, 4021-4035. doi: 10.1529/biophysj.104.050765.
    • (2004) Biophysical Journal , vol.87 , pp. 4021-4035
    • Slutsky, M.1    Mirny, L.A.2
  • 186
    • 76249126156 scopus 로고    scopus 로고
    • Multiple native states reveal persistent ruggedness of an RNA folding landscape
    • SOLOMATIN, S. V., GREENFELD, M., CHU, S. & HERSCHLAG, D. (2010). Multiple native states reveal persistent ruggedness of an RNA folding landscape. Nature 463, 681-684. doi: 10.1038/nature08717.
    • (2010) Nature , vol.463 , pp. 681-684
    • Solomatin, S.V.1    Greenfeld, M.2    Chu, S.3    Herschlag, D.4
  • 187
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • SPOLAR, R. S. & RECORD, M. T. Jr (1994). Coupling of local folding to site-specific binding of proteins to DNA. Science 263, 777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 189
    • 58149464544 scopus 로고    scopus 로고
    • Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape
    • STREET, T.O. & BARRICK, D. (2009). Predicting repeat protein folding kinetics from an experimentally determined folding energy landscape. Protein Science 18, 58-68. doi: 10.1002/pro.9.
    • (2009) Protein Science , vol.18 , pp. 58-68
    • Street, T.O.1    Barrick, D.2
  • 192
    • 84855599223 scopus 로고    scopus 로고
    • Designed ankyrin repeat proteins (DARPins) from research to therapy
    • TAMASKOVIC, R., SIMON, M., STEFAN, N., SCHWILL, M. & PLÜCKTHUN, A. (2012). Designed ankyrin repeat proteins (DARPins) from research to therapy. Methods in Enzymology 503, 101-134. doi: 10.1016/B978-0-12-396962-0.00005-7.
    • (2012) Methods in Enzymology , vol.503 , pp. 101-134
    • Tamaskovic, R.1    Simon, M.2    Stefan, N.3    Schwill, M.4    Plückthun, A.5
  • 196
    • 70349901079 scopus 로고    scopus 로고
    • Stability effects of mutations and protein evolvability
    • TOKURIKI, N. & TAWFIK, D. S. (2009). Stability effects of mutations and protein evolvability. Currunet Opinion in Structural Biology 19, 596-604. doi: 10.1016/j.sbi.2009.08.003.
    • (2009) Currunet Opinion in Structural Biology , vol.19 , pp. 596-604
    • Tokuriki, N.1    Tawfik, D.S.2
  • 197
    • 42649092133 scopus 로고    scopus 로고
    • Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape
    • TRIPP, K.W. & BARRICK, D. (2008). Rerouting the folding pathway of the Notch ankyrin domain by reshaping the energy landscape. Journal of the American Chemical Society 130, 5681-5688. doi: 10.1021/ja0763201.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 5681-5688
    • Tripp, K.W.1    Barrick, D.2
  • 198
    • 84885460398 scopus 로고    scopus 로고
    • Funneling and frustration in the energy landscapes of some designed and simplified proteins
    • TRUONG, H. H., KIM, B. L., SCHAFER, N.P. & WOLYNES, P. G. (2013). Funneling and frustration in the energy landscapes of some designed and simplified proteins. Journal of Chemical Physics 139, 121908.
    • (2013) Journal of Chemical Physics , vol.139 , pp. 121908
    • Truong, H.H.1    Kim, B.L.2    Schafer, N.P.3    Wolynes, P.G.4
  • 199
    • 57649219476 scopus 로고    scopus 로고
    • The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry
    • TSUTSUI, Y., KURI, B., SENGUPTA, T. & WINTRODE, P.L. (2008). The structural basis of serpin polymerization studied by hydrogen/deuterium exchange and mass spectrometry. Journal of Biological Chemistry 283, 30804-30811. doi: 10.1074/jbc.M804048200.
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 30804-30811
    • Tsutsui, Y.1    Kuri, B.2    Sengupta, T.3    Wintrode, P.L.4
  • 200
    • 0009791166 scopus 로고
    • Theory of the frustration effect. II. Ising spins on a square lattice
    • VANNIMENUS, J. & TOULOUSE, G. (1977). Theory of the frustration effect. II. Ising spins on a square lattice. Journal of Physics C: Solid State Physics 10, L537. URL: http://stacks.iop.org/0022-3719/10/i=18/a=008.
    • (1977) Journal of Physics C: Solid State Physics , vol.10 , pp. L537
    • Vannimenus, J.1    Toulouse, G.2
  • 201
    • 31544474375 scopus 로고    scopus 로고
    • DNA nanomechanical switches under folding kinetics control
    • VIASNOFF, V., MELLER, A. & ISAMBERT, H. (2006). DNA nanomechanical switches under folding kinetics control. Nano Letters 6, 101-104. doi: 10.1021/n105216c.
    • (2006) Nano Letters , vol.6 , pp. 101-104
    • Viasnoff, V.1    Meller, A.2    Isambert, H.3
  • 203
    • 0000460062 scopus 로고    scopus 로고
    • Symmetry, near-symmetry and energetics
    • WALES, D. J. (1998). Symmetry, near-symmetry and energetics. Chemical Physics Letters 285, 330-336.
    • (1998) Chemical Physics Letters , vol.285 , pp. 330-336
    • Wales, D.J.1
  • 205
    • 36149010740 scopus 로고
    • Antiferromagnetism
    • WANNIER, G. H. (1950a). Antiferromagnetism. The Triangular Ising Net. Physical Review 79, 357-364. doi: 10.1103/PhysRev.79.357. URL: http://link.aps.org/doi /10.1103/PhysRev.79.357
    • (1950) The Triangular Ising Net. Physical Review , vol.79 , pp. 357-364
    • Wannier, G.H.1
  • 206
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids
    • WATSON, J.D. & CRICK, F. H. C. (1953). Molecular structure of nucleic acids. Nature 171, 737-738.
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 207
    • 64849115340 scopus 로고    scopus 로고
    • Chemical frustration in the protein folding landscape: Grand canonical ensemble simulations of cytochrome c
    • WEINKAM, P., ROMESBERG, F.E. & WOLYNES, P.G. (2009). Chemical frustration in the protein folding landscape: grand canonical ensemble simulations of cytochrome c. Biochemistry 48, 2394-2402. doi: 10.1021/bi802293m.
    • (2009) Biochemistry , vol.48 , pp. 2394-2402
    • Weinkam, P.1    Romesberg, F.E.2    Wolynes, P.G.3
  • 208
    • 84910148675 scopus 로고    scopus 로고
    • The folding landscapes of metalloproteins; in protein folding and metal ions: Mechanisms, biology and disease
    • (eds. P. WITTUNG-STAFSHED & M.C. GOMES) Boca Raton, FL: Taylor and Francis
    • WEINKAM, P. & WOLYNES, P. G. (2010a). The folding landscapes of metalloproteins; in protein folding and metal ions: mechanisms, biology and disease. In Protein Folding and Metal Ions: Mechanisms, Biology and Disease (eds. P. WITTUNG-STAFSHED & M.C. GOMES) pp. 247-273. Boca Raton, FL: Taylor and Francis.
    • (2010) Protein Folding and Metal Ions: Mechanisms, Biology and Disease , pp. 247-273
    • Weinkam, P.1    Wolynes, P.G.2
  • 209
    • 77952590099 scopus 로고    scopus 로고
    • The folding energy landscape and free energy excitations of cytochrome c
    • WEINKAM, P., ZIMMERMANN, J., ROMESBERG, F.E. & WOLYNES, P. G. (2010b). The folding energy landscape and free energy excitations of cytochrome c. Accounts of Chemical Research 43, 652-660. doi: 10.1021/ar9002703.
    • (2010) Accounts of Chemical Research , vol.43 , pp. 652-660
    • Weinkam, P.1    Zimmermann, J.2    Romesberg, F.E.3    Wolynes, P.G.4
  • 210
    • 58149171911 scopus 로고    scopus 로고
    • Characterization of alkaline transitions in ferricytochrome c using carbon-deuterium infrared probes
    • WEINKAM, P., ZIMMERMANN, J., SAGLE, L. B., MATSUDA, S., DAWSON, P. E., WOLYNES, P.G. & ROMESBERG, F.E. (2008). Characterization of alkaline transitions in ferricytochrome c using carbon-deuterium infrared probes. Biochemistry 47, 13470-13480. doi: 10.1021/bi801223n.
    • (2008) Biochemistry , vol.47 , pp. 13470-13480
    • Weinkam, P.1    Zimmermann, J.2    Sagle, L.B.3    Matsuda, S.4    Dawson, P.E.5    Wolynes, P.G.6    Romesberg, F.E.7
  • 211
    • 24644481440 scopus 로고    scopus 로고
    • A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments
    • WEINKAM, P., ZONG, C. & WOLYNES, P. G. (2005). A funneled energy landscape for cytochrome c directly predicts the sequential folding route inferred from hydrogen exchange experiments. Proceedings of the National Academy of Sciences of the United States of America 102, 12401-12406. doi: 10.1073/pnas.0505274102.
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , pp. 12401-12406
    • Weinkam, P.1    Zong, C.2    Wolynes, P.G.3
  • 212
    • 84878934226 scopus 로고    scopus 로고
    • Diabetes mellitus due to the toxic misfolding of proinsulin variants
    • WEISS, M. A. (2013). Diabetes mellitus due to the toxic misfolding of proinsulin variants. FEBS Letters 587, 1942-1950. doi: 10.1016/j.febslet.2013.04.044.
    • (2013) FEBS Letters , vol.587 , pp. 1942-1950
    • Weiss, M.A.1
  • 214
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • WEISSMAN, J.S. & KIM, P. S. (1991). Reexamination of the folding of BPTI: predominance of native intermediates. Science 253, 1386-1393.
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 216
    • 76249117417 scopus 로고    scopus 로고
    • Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family
    • WENSLEY, B. G., BATEY, S., BONE, F. A. C., CHAN, Z. M., TUMELTY, N. R., STEWARD, A., KWA, L. G., BORGIA, A. & CLARKE, J. (2010). Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family. Nature 463, 685-688. doi: 10.1038/nature08743.
    • (2010) Nature , vol.463 , pp. 685-688
    • Wensley, B.G.1    Batey, S.2    Bone, F.A.C.3    Chan, Z.M.4    Tumelty, N.R.5    Steward, A.6    Kwa, L.G.7    Borgia, A.8    Clarke, J.9
  • 220
    • 61949448788 scopus 로고    scopus 로고
    • Energy landscape along an enzymatic reaction trajectory: Hinges or cracks?
    • WHITFORD, P. C., ONUCHIC, J.N. & WOLYNES, P. G. (2008). Energy landscape along an enzymatic reaction trajectory: hinges or cracks? HFSP Journal 2, 61-64. doi: 10.2976/1.2894846.
    • (2008) HFSP Journal , vol.2 , pp. 61-64
    • Whitford, P.C.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 221
    • 82555168273 scopus 로고    scopus 로고
    • NMR characterisation of the relationship between frustration and the excited state of IM7
    • WHITTAKER, S. B-M, CLAYDEN, N.J. & MOORE, G.R. (2011). NMR characterisation of the relationship between frustration and the excited state of IM7. Journal of Molecular Biology 414, 511-529. doi: 10.1016/j.jmb.2011.09.038.
    • (2011) Journal of Molecular Biology , vol.414 , pp. 511-529
    • Whittaker, S.B.-M.1    Clayden, N.J.2    Moore, G.R.3
  • 222
    • 0032544188 scopus 로고    scopus 로고
    • Interactions of phenol and m-cresol in the insulin hexamer, and their effect on the association properties of B28 pro - Asp insulin analogues
    • WHITTINGHAM, J. L., EDWARDS, D. J., ANTSON, A. A., CLARKSON, J.M. & DODSON, G. G. (1998). Interactions of phenol and m-cresol in the insulin hexamer, and their effect on the association properties of B28 pro - Asp insulin analogues. Biochemistry 37, 11516-11523. doi: 10.1021/bi980807s.
    • (1998) Biochemistry , vol.37 , pp. 11516-11523
    • Whittingham, J.L.1    Edwards, D.J.2    Antson, A.A.3    Clarkson, J.M.4    Dodson, G.G.5
  • 228
    • 33750970551 scopus 로고    scopus 로고
    • Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid
    • WOODSIDE, M. T., ANTHONY, P. C., BEHNKE-PARKS, W. M., LARIZADEH, K., HERSCHLAG, D. & BLOCK, S.M. (2006). Direct measurement of the full, sequence-dependent folding landscape of a nucleic acid. Science 314, 1001-1004. doi: 10.1126/science.1133601.
    • (2006) Science , vol.314 , pp. 1001-1004
    • Woodside, M.T.1    Anthony, P.C.2    Behnke-Parks, W.M.3    Larizadeh, K.4    Herschlag, D.5    Block, S.M.6
  • 229
    • 28644437048 scopus 로고    scopus 로고
    • The importance of sequence diversity in the aggregation and evolution of proteins
    • WRIGHT, C. F., TEICHMANN, S. A., CLARKE, J. & DOBSON, C.M. (2005). The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438, 878-881. doi: 10.1038/nature04195.
    • (2005) Nature , vol.438 , pp. 878-881
    • Wright, C.F.1    Teichmann, S.A.2    Clarke, J.3    Dobson, C.M.4
  • 230
    • 84893777301 scopus 로고    scopus 로고
    • Designing cooperativity into the designed protein Top7
    • YADAHALLI, S. & GOSAVI, S. (2014). Designing cooperativity into the designed protein Top7. Proteins 82, 364-374. doi: 10.1002/prot.24393.
    • (2014) Proteins , vol.82 , pp. 364-374
    • Yadahalli, S.1    Gosavi, S.2
  • 231
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • YAMASAKI, M., LI, W., JOHNSON, D.J.D. & HUNTINGTON, J. A. (2008). Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455, 1255-1258. doi: 10.1038/nature07394.
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.D.3    Huntington, J.A.4
  • 233
    • 0037379184 scopus 로고    scopus 로고
    • Structural and kinetic characterization of the simplified SH3 domain FP1
    • YI, Q., RAJAGOPAL, P., KLEVIT, R.E. & BAKER, D. (2003). Structural and kinetic characterization of the simplified SH3 domain FP1. Protein Science 12, 776-783. doi: 10.1110/ps.0238603.
    • (2003) Protein Science , vol.12 , pp. 776-783
    • Yi, Q.1    Rajagopal, P.2    Klevit, R.E.3    Baker, D.4
  • 235
    • 84872283908 scopus 로고    scopus 로고
    • Analysis of 15N-1H NMR relaxation in proteins by a combined experimental and molecular dynamics simulation approach: Picosecond-nanosecond dynamics of the Rho GTPase binding domain of plexin-b1 in the dimeric state indicates allosteric pathways
    • ZERBETTO, M., ANDERSON, R., BOUGUET-BONNET, S., RECH, M., ZHANG, L., MEIROVITCH, E., POLIMENO, A. & BUCK, M. (2013). Analysis of 15N-1H NMR relaxation in proteins by a combined experimental and molecular dynamics simulation approach: picosecond-nanosecond dynamics of the Rho GTPase binding domain of plexin-b1 in the dimeric state indicates allosteric pathways. Journal of Physical Chemistry B 117, 174-184. doi: 10.1021/jp310142f.
    • (2013) Journal of Physical Chemistry B , vol.117 , pp. 174-184
    • Zerbetto, M.1    Anderson, R.2    Bouguet-Bonnet, S.3    Rech, M.4    Zhang, L.5    Meirovitch, E.6    Polimeno, A.7    Buck, M.8
  • 236
    • 0031577566 scopus 로고    scopus 로고
    • Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites
    • ZHANG, H. J., SHENG, X. R., PAN, X.M. & ZHOU, J.M. (1997). Activation of adenylate kinase by denaturants is due to the increasing conformational flexibility at its active sites. Biochemical and Biophysical Research Communications 238, 382-386. doi: 10.1006/bbrc.1997.7301.
    • (1997) Biochemical and Biophysical Research Communications , vol.238 , pp. 382-386
    • Zhang, H.J.1    Sheng, X.R.2    Pan, X.M.3    Zhou, J.M.4
  • 237
    • 0043102513 scopus 로고    scopus 로고
    • A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis
    • ZHANG, X-J, BAASE, W.A. & MATTHEWS, B.W. (2002). A helix initiation signal in T4 lysozyme identified by polyalanine mutagenesis. Biophysical Chemistry 101-102, 43-56.
    • (2002) Biophysical Chemistry 101-102 , pp. 43-56
    • Zhang, X.-J.1    Baase, W.A.2    Matthews, B.W.3
  • 238
    • 77649264931 scopus 로고    scopus 로고
    • Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins
    • ZHANG, Z. & CHAN, H. S. (2010). Competition between native topology and nonnative interactions in simple and complex folding kinetics of natural and designed proteins. Proceedings of the National Academy of Sciences of the United States of America 107, 2920-2925.
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , pp. 2920-2925
    • Zhang, Z.1    Chan, H.S.2
  • 241
    • 0000668407 scopus 로고
    • Theory of the phase transition between helix and random coil in polypeptide chains
    • ZIMM, B.H. & BRAGG, J. K. (1959). Theory of the phase transition between helix and random coil in polypeptide chains. Journal of Chemical Physics 31, 526.
    • (1959) Journal of Chemical Physics , vol.31 , pp. 526
    • Zimm, B.H.1    Bragg, J.K.2
  • 242
    • 33646866548 scopus 로고    scopus 로고
    • φ-Value analysis of apo-azurin folding: Comparison between experiment and theory
    • ZONG, C., WILSON, C. J., SHEN, T., WOLYNES, P.G. & WITTUNG-STAFSHEDE, P. (2006). φ-Value analysis of apo-azurin folding: comparison between experiment and theory. Biochemistry 45, 6458-6466.
    • (2006) Biochemistry , vol.45 , pp. 6458-6466
    • Zong, C.1    Wilson, C.J.2    Shen, T.3    Wolynes, P.G.4    Wittung-Stafshede, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.