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Volumn 36, Issue , 2007, Pages 261-280

Physics of proteins

Author keywords

Amyloid; Geometry; Marginally compact phase; Symmetry; Tube

Indexed keywords

AMYLOID;

EID: 34347206296     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.36.040306.132808     Document Type: Review
Times cited : (71)

References (78)
  • 1
    • 34247953814 scopus 로고
    • More is different: Broken symmetry and nature of hierarchical structure of science
    • Anderson PW. 1972. More is different: broken symmetry and nature of hierarchical structure of science. Science 177:393-96
    • (1972) Science , vol.177 , pp. 393-396
    • Anderson, P.W.1
  • 2
    • 0020769932 scopus 로고
    • Suggested model for prebiotic evolution: The use of chaos
    • Anderson PW. 1983. Suggested model for prebiotic evolution: the use of chaos. Proc. Natl. Acad. Sci. USA 80:3386-90
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3386-3390
    • Anderson, P.W.1
  • 3
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen CB. 1973. Principles that govern folding of protein chains. Science 181:223-30
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 34347226009 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 5
    • 34347271038 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 6
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D. 2000. A surprising simplicity to protein folding. Nature 405:39-42
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 10
    • 0035283155 scopus 로고    scopus 로고
    • Computational approach to the protein-folding problem
    • Banavar JR, Maritan A. 2001. Computational approach to the protein-folding problem. Proteins 42:433-35
    • (2001) Proteins , vol.42 , pp. 433-435
    • Banavar, J.R.1    Maritan, A.2
  • 11
    • 0037847500 scopus 로고    scopus 로고
    • Colloquium: Geometrical approach to protein folding: a tube picture
    • Banavar JR, Maritan A. 2003. Colloquium: geometrical approach to protein folding: a tube picture. Rev. Mod. Phys. 75:23-34
    • (2003) Rev. Mod. Phys , vol.75 , pp. 23-34
    • Banavar, J.R.1    Maritan, A.2
  • 13
    • 0011429211 scopus 로고
    • Structure of proteins
    • Bernal JD. 1939. Structure of proteins. Nature 143:663-67
    • (1939) Nature , vol.143 , pp. 663-667
    • Bernal, J.D.1
  • 14
    • 0025363984 scopus 로고
    • Deciphering the message in protein sequences: Tolerance to amino acid substitutions
    • Bowie JU, Reidhaar-Olson JF, Lim WA, Sauer RT. 1990. Deciphering the message in protein sequences: tolerance to amino acid substitutions. Science 247:1306-10
    • (1990) Science , vol.247 , pp. 1306-1310
    • Bowie, J.U.1    Reidhaar-Olson, J.F.2    Lim, W.A.3    Sauer, R.T.4
  • 16
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein-folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG. 1995. Funnels, pathways, and the energy landscape of protein-folding: a synthesis. Proteins 21:167-95
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 17
    • 0023449962 scopus 로고
    • Spin-glasses and the statistical mechanics of protein folding
    • Bryngelson JD, Wolynes PG. 1987. Spin-glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. USA 84:7524-28
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 19
    • 0025150383 scopus 로고
    • Origins of structure in globular proteins
    • Chan HS, Dill KA. 1990. Origins of structure in globular proteins. Proc. Natl. Acad. Sci. USA 87:6388-92
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6388-6392
    • Chan, H.S.1    Dill, K.A.2
  • 20
    • 0000868733 scopus 로고
    • The protein folding problem
    • Chan HS, Dill KA. 1993. The protein folding problem. Phys. Today 46:24-32
    • (1993) Phys. Today , vol.46 , pp. 24-32
    • Chan, H.S.1    Dill, K.A.2
  • 21
    • 0027122748 scopus 로고
    • Proteins: 1000 families for the molecular biologist
    • Chothia C. 1992. Proteins: 1000 families for the molecular biologist. Nature 357:543-44
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 22
    • 0025277191 scopus 로고
    • The classifications and origins of protein folding patterns
    • Chothia C, Finkelstein AV. 1990. The classifications and origins of protein folding patterns. Annu. Rev. Biochem. 59:1007-39
    • (1990) Annu. Rev. Biochem , vol.59 , pp. 1007-1039
    • Chothia, C.1    Finkelstein, A.V.2
  • 26
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat BI, Mayo SL. 1997. De novo protein design: fully automated sequence selection. Science 278:82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 27
    • 0028218304 scopus 로고
    • Folded proteins occur frequently in libraries of random amino acid sequences
    • Davidson AR, Sauer RT. 1994. Folded proteins occur frequently in libraries of random amino acid sequences. Proc. Natl. Acad. Sci. USA 91:2146-50
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2146-2150
    • Davidson, A.R.1    Sauer, R.T.2
  • 29
  • 30
    • 0035932508 scopus 로고    scopus 로고
    • Laws of form revisited
    • Denton M, Marshall C. 2001. Laws of form revisited. Nature 410:417-17
    • (2001) Nature , vol.410 , pp. 417-417
    • Denton, M.1    Marshall, C.2
  • 31
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS. 1997. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4:10-19
    • (1997) Nat. Struct. Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 32
    • 0037317334 scopus 로고    scopus 로고
    • Dobson CM. 2003. Protein folding and disease: a view from the first Horizon Symposium. Nat. Rev. Drug Discov. 2:154-60
    • Dobson CM. 2003. Protein folding and disease: a view from the first Horizon Symposium. Nat. Rev. Drug Discov. 2:154-60
  • 34
    • 0141480054 scopus 로고    scopus 로고
    • Funnel sculpting for in silico assembly of secondary structure elements of proteins
    • Fain B, Levitt M. 2003. Funnel sculpting for in silico assembly of secondary structure elements of proteins. Proc. Natl. Acad. Sci. USA 100:10700-5
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10700-10705
    • Fain, B.1    Levitt, M.2
  • 39
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Gō N. 1983. Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12:183-210
    • (1983) Annu. Rev. Biophys. Bioeng , vol.12 , pp. 183-210
    • Gō, N.1
  • 41
    • 0025040232 scopus 로고
    • De novo design, expression, and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht MH, Richardson JS, Richardson DC, Ogden RC. 1990. De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence. Science 249:884-91
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.H.1    Richardson, J.S.2    Richardson, D.C.3    Ogden, R.C.4
  • 42
    • 0026552361 scopus 로고
    • Folding and function of a t4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence
    • Heinz DW, Baase WA, Matthews BW. 1992. Folding and function of a t4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. Proc. Natl. Acad. Sci. USA 89:3751-55
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3751-3755
    • Heinz, D.W.1    Baase, W.A.2    Matthews, B.W.3
  • 46
    • 0031000649 scopus 로고    scopus 로고
    • An evolutionary treasure: Unification of a broad set of amidohydrolases related to urease
    • Holm L, Sander C. 1997. An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Proteins 28:72-82
    • (1997) Proteins , vol.28 , pp. 72-82
    • Holm, L.1    Sander, C.2
  • 47
    • 0020118274 scopus 로고
    • Neural networks and physical systems with emergent collective computational abilities
    • Hopfield JJ. 1982. Neural networks and physical systems with emergent collective computational abilities. Proc. Natl. Acad. Sci. USA 79:2554-58
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 2554-2558
    • Hopfield, J.J.1
  • 49
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar S, Schiffer JM, Xiong HY, Babik JM, Hecht MH. 1993. Protein design by binary patterning of polar and nonpolar amino acids. Science 262:1680-85
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.Y.3    Babik, J.M.4    Hecht, M.H.5
  • 52
    • 0025908265 scopus 로고
    • The role of internal packing interactions in determining the structure and stability of a protein
    • Lim WA, Sauer RT. 1991. The role of internal packing interactions in determining the structure and stability of a protein. J. Mol. Biol. 219:359-76
    • (1991) J. Mol. Biol , vol.219 , pp. 359-376
    • Lim, W.A.1    Sauer, R.T.2
  • 53
    • 0001181898 scopus 로고    scopus 로고
    • United-residue force field for off-lattice protein-structure simulations. III. Origin of backbone hydrogen-bonding cooperativity in united-residue potentials
    • Liwo A, Kazmierkiewicz R, Czaplewski C, Groth M, Oldziej S, et al. 1998. United-residue force field for off-lattice protein-structure simulations. III. Origin of backbone hydrogen-bonding cooperativity in united-residue potentials. J. Comput. Chem. 19:259-76
    • (1998) J. Comput. Chem , vol.19 , pp. 259-276
    • Liwo, A.1    Kazmierkiewicz, R.2    Czaplewski, C.3    Groth, M.4    Oldziej, S.5
  • 56
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews BW. 1993. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62:139-60
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 58
    • 0029063717 scopus 로고
    • The complexity and accuracy of discrete state models of protein structure
    • Park B, Levitt M. 1995. The complexity and accuracy of discrete state models of protein structure. J. Mol. Biol. 249:493-507
    • (1995) J. Mol. Biol , vol.249 , pp. 493-507
    • Park, B.1    Levitt, M.2
  • 59
    • 0000573263 scopus 로고
    • Configurations of polypeptide chains with favored orientations around single bonds: Two new pleated sheets
    • Pauling L, Corey RB. 1951. Configurations of polypeptide chains with favored orientations around single bonds: two new pleated sheets. Proc. Natl. Acad. Sci. USA 37:729-40
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 729-740
    • Pauling, L.1    Corey, R.B.2
  • 60
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling L, Corey RB, Branson HR. 1951. The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc. Natl. Acad. Sci. USA 37:205-11
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 65
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander C, Schneider R. 1991. Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9:56-68
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 66
    • 0014935646 scopus 로고
    • Natural selection and concept of a protein space
    • Smith JM. 1970. Natural selection and concept of a protein space. Nature 225:563-63
    • (1970) Nature , vol.225 , pp. 563-563
    • Smith, J.M.1
  • 68
    • 0033405203 scopus 로고    scopus 로고
    • A physical basis for protein secondary structure
    • Srinivasan R, Rose GD. 1999. A physical basis for protein secondary structure. Proc. Natl. Acad. Sci. USA 96:14258-63
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14258-14263
    • Srinivasan, R.1    Rose, G.D.2
  • 69
    • 0034691422 scopus 로고    scopus 로고
    • Mathematics: Best packing in proteins and DNA
    • Stasiak A, Maddocks JH. 2000. Mathematics: best packing in proteins and DNA. Nature 406:251-53
    • (2000) Nature , vol.406 , pp. 251-253
    • Stasiak, A.1    Maddocks, J.H.2
  • 72
    • 0037161731 scopus 로고    scopus 로고
    • Comparative assessment of large-scale data sets of protein-protein interactions
    • von Mering C, Krause R, Snel B, Cornell M, Oliver SG, et al. 2002. Comparative assessment of large-scale data sets of protein-protein interactions. Nature 417:399-403
    • (2002) Nature , vol.417 , pp. 399-403
    • von Mering, C.1    Krause, R.2    Snel, B.3    Cornell, M.4    Oliver, S.G.5
  • 73
    • 0038497542 scopus 로고
    • Molecular structure of nucleic acids: A structure for deoxyribose nucleic acid
    • Watson JD, Crick FHC. 1953. Molecular structure of nucleic acids: a structure for deoxyribose nucleic acid. Nature 171:737-38
    • (1953) Nature , vol.171 , pp. 737-738
    • Watson, J.D.1    Crick, F.H.C.2
  • 74
    • 0344392714 scopus 로고    scopus 로고
    • Solution structure of a de novo protein from a designed combinatorial library
    • Wei Y, Kim S, Fela D, Baum J, Hecht MH. 2003. Solution structure of a de novo protein from a designed combinatorial library. Proc. Natl. Acad. Sci. USA 100:13270-73
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13270-13273
    • Wei, Y.1    Kim, S.2    Fela, D.3    Baum, J.4    Hecht, M.H.5
  • 78
    • 19744382834 scopus 로고    scopus 로고
    • Entropically driven helix formation
    • Snir Y, Kamien RD. 2005. Entropically driven helix formation. Science 307:1067
    • (2005) Science , vol.307 , pp. 1067
    • Snir, Y.1    Kamien, R.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.