메뉴 건너뛰기




Volumn 14, Issue 6, 2006, Pages 1059-1072

Sequence and Structure Analysis of Parallel β Helices: Implication for Constructing Amyloid Structural Models

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; AMYLOID; ASPARAGINE; CYSTEINE; PHENYLALANINE; POLYPEPTIDE; PROLINE;

EID: 33744807442     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.03.015     Document Type: Article
Times cited : (38)

References (65)
  • 1
    • 4644296906 scopus 로고    scopus 로고
    • Anatomy of an amyloidogenic intermediate: Conversion of β-sheet to α-sheet structure in transthyretin at acidic pH
    • Armen R.S., Alonso D.O.V., and Daggett V. Anatomy of an amyloidogenic intermediate: Conversion of β-sheet to α-sheet structure in transthyretin at acidic pH. Structure 12 (2004) 1847-1863
    • (2004) Structure , vol.12 , pp. 1847-1863
    • Armen, R.S.1    Alonso, D.O.V.2    Daggett, V.3
  • 2
    • 4143067019 scopus 로고    scopus 로고
    • Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease
    • Armen R.S., DeMarco M.L., Alonso D.O.V., and Daggett V. Pauling and Corey's α-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proc. Natl. Acad. Sci. USA 101 (2004) 11622-11627
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11622-11627
    • Armen, R.S.1    DeMarco, M.L.2    Alonso, D.O.V.3    Daggett, V.4
  • 3
    • 0035823520 scopus 로고    scopus 로고
    • Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation
    • Azriel R., and Gazit E. Analysis of the minimal amyloid-forming fragment of the islet amyloid polypeptide. An experimental support for the key role of the phenylalanine residue in amyloid formation. J. Biol. Chem. 276 (2001) 34156-34161
    • (2001) J. Biol. Chem. , vol.276 , pp. 34156-34161
    • Azriel, R.1    Gazit, E.2
  • 5
    • 0035956924 scopus 로고    scopus 로고
    • An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid
    • Balbirnie M., Grothe R., and Eisenberg D.S. An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid. Proc. Natl. Acad. Sci. USA 98 (2001) 2375-2380
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2375-2380
    • Balbirnie, M.1    Grothe, R.2    Eisenberg, D.S.3
  • 6
    • 0038004726 scopus 로고    scopus 로고
    • β(2)-microglobulin amyloidosis: insights from conservation analysis and fibril modelling by protein docking techniques
    • Benyamini H., Gunasekaran K., Wolfson H., and Nussinov R. β(2)-microglobulin amyloidosis: insights from conservation analysis and fibril modelling by protein docking techniques. J. Mol. Biol. 330 (2003) 159-174
    • (2003) J. Mol. Biol. , vol.330 , pp. 159-174
    • Benyamini, H.1    Gunasekaran, K.2    Wolfson, H.3    Nussinov, R.4
  • 8
    • 0035833997 scopus 로고    scopus 로고
    • An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates parallel β-fibrils
    • Bevivino A.E., and Loll P.J. An expanded glutamine repeat destabilizes native ataxin-3 structure and mediates parallel β-fibrils. Proc. Natl. Acad. Sci. USA 98 (2001) 11955-11960
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11955-11960
    • Bevivino, A.E.1    Loll, P.J.2
  • 9
    • 0033869715 scopus 로고    scopus 로고
    • Endocytic pathway abnormalities precede amyloid β deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations
    • Cataldo A.M., Peterhoff C.M., Troncoso J.C., Gomez-Isla T., Hyman B.T., and Nixon R.A. Endocytic pathway abnormalities precede amyloid β deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am. J. Pathol. 157 (2000) 277-286
    • (2000) Am. J. Pathol. , vol.157 , pp. 277-286
    • Cataldo, A.M.1    Peterhoff, C.M.2    Troncoso, J.C.3    Gomez-Isla, T.4    Hyman, B.T.5    Nixon, R.A.6
  • 10
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • Chiti F., Stefani M., Taddei N., Ramponi G., and Dobson C.M. Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424 (2003) 805-808
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 11
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou P.Y., and Fasman G.D. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47 (1978) 251-276
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 12
    • 0033455572 scopus 로고    scopus 로고
    • Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid
    • Deane C.M., Allen F.H., Taylor R., and Blundell T.L. Carbonyl-carbonyl interactions stabilize the partially allowed Ramachandran conformations of asparagine and aspartic acid. Protein Eng. 12 (1999) 1025-1028
    • (1999) Protein Eng. , vol.12 , pp. 1025-1028
    • Deane, C.M.1    Allen, F.H.2    Taylor, R.3    Blundell, T.L.4
  • 13
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: protofibril formation of the prion protein
    • DeMarco M.L., and Daggett V. From conversion to aggregation: protofibril formation of the prion protein. Proc. Natl. Acad. Sci. USA 101 (2004) 2293-2298
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2293-2298
    • DeMarco, M.L.1    Daggett, V.2
  • 14
    • 0037317334 scopus 로고    scopus 로고
    • Protein folding and disease: a view from the first Horizon Symposium
    • Dobson C.M. Protein folding and disease: a view from the first Horizon Symposium. Nat. Rev. Drug Discov. 2 (2003) 154-160
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 154-160
    • Dobson, C.M.1
  • 15
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson C.M. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 15 (2004) 3-16
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 16
    • 20444437608 scopus 로고    scopus 로고
    • Structural biology: prying into prions
    • Dobson C.M. Structural biology: prying into prions. Nature 435 (2005) 747-749
    • (2005) Nature , vol.435 , pp. 747-749
    • Dobson, C.M.1
  • 17
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich M., and Dobson C.M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21 (2002) 5682-5690
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 18
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin: even an ordinary globular protein can assume a rogue guise if conditions are right
    • Fandrich M., Fletcher M.A., and Dobson C.M. Amyloid fibrils from muscle myoglobin: even an ordinary globular protein can assume a rogue guise if conditions are right. Nature 410 (2001) 165-166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 19
    • 0000484499 scopus 로고
    • Hydrophobic parameters-pi of amino-acid side-chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere J.L., and Pliska V. Hydrophobic parameters-pi of amino-acid side-chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. 18 (1983) 369-375
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 20
    • 0036135139 scopus 로고    scopus 로고
    • A possible role for π-stacking in the self-assembly of amyloid fibrils
    • Gazit E. A possible role for π-stacking in the self-assembly of amyloid fibrils. FASEB J. 16 (2002) 77-83
    • (2002) FASEB J. , vol.16 , pp. 77-83
    • Gazit, E.1
  • 21
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts C., Wille H., Prusiner S.B., and Cohen F.E. Evidence for assembly of prions with left-handed β-helices into trimers. Proc. Natl. Acad. Sci. USA 101 (2004) 8342-8347
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 22
    • 0031455857 scopus 로고    scopus 로고
    • β-hairpins in proteins revisited: lessons for de novo design
    • Gunasekaran K., Ramakrishnan C., and Balaram P. β-hairpins in proteins revisited: lessons for de novo design. Protein Eng. 10 (1997) 1131-1141
    • (1997) Protein Eng. , vol.10 , pp. 1131-1141
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 23
    • 0032488824 scopus 로고    scopus 로고
    • Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals
    • Gunasekaran K., Nagarajaram H.A., Ramakrishnan C., and Balaram P. Stereochemical punctuation marks in protein structures: glycine and proline containing helix stop signals. J. Mol. Biol. 275 (1998) 917-932
    • (1998) J. Mol. Biol. , vol.275 , pp. 917-932
    • Gunasekaran, K.1    Nagarajaram, H.A.2    Ramakrishnan, C.3    Balaram, P.4
  • 24
    • 4544335325 scopus 로고    scopus 로고
    • Molecular modeling of the core of Aβ amyloid fibrils
    • Guo J.-T., Wetzel R., and Xu Y. Molecular modeling of the core of Aβ amyloid fibrils. Proteins 57 (2004) 357-364
    • (2004) Proteins , vol.57 , pp. 357-364
    • Guo, J.-T.1    Wetzel, R.2    Xu, Y.3
  • 27
    • 3242735504 scopus 로고    scopus 로고
    • An amyloid-forming segment of β 2-microglobulin suggests a molecular model for the fibril
    • Ivanova M.I., Sawaya M.R., Gingery M., Attinger A., and Eisenberg D. An amyloid-forming segment of β 2-microglobulin suggests a molecular model for the fibril. Proc. Natl. Acad. Sci. USA 101 (2004) 10584-10589
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10584-10589
    • Ivanova, M.I.1    Sawaya, M.R.2    Gingery, M.3    Attinger, A.4    Eisenberg, D.5
  • 28
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec C.P., MacPhee C.E., Bajaj V.S., McMahon M.T., Dobson C.M., and Griffin R.G. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc. Natl. Acad. Sci. USA 101 (2004) 711-716
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5    Griffin, R.G.6
  • 29
    • 0035543109 scopus 로고    scopus 로고
    • The architecture of parallel β-helices and related folds
    • Jenkins J., and Pickersgill R. The architecture of parallel β-helices and related folds. Prog. Biophys. Mol. Biol. 77 (2001) 111-175
    • (2001) Prog. Biophys. Mol. Biol. , vol.77 , pp. 111-175
    • Jenkins, J.1    Pickersgill, R.2
  • 30
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • Jimenez J.L., Guijarro J.L., Orlova E., Zurdo J., Dobson C.M., Sunde M., and Saibil H.R. Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. EMBO J. 18 (1999) 815-821
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.L.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 32
    • 33744796051 scopus 로고    scopus 로고
    • Computational prediction of protein phosphopeptide-binding sites
    • Joughin B.A., Yaffe M.B., and Tidor B. Computational prediction of protein phosphopeptide-binding sites. Protein Sci. 13 (2004) 146
    • (2004) Protein Sci. , vol.13 , pp. 146
    • Joughin, B.A.1    Yaffe, M.B.2    Tidor, B.3
  • 33
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: the parallel superpleated β-structure
    • Kajava A.V., Baxa U., Wickner R.B., and Steven A.C. A model for Ure2p prion filaments and other amyloids: the parallel superpleated β-structure. Proc. Natl. Acad. Sci. USA 101 (2004) 7885-7890
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 34
    • 0034492510 scopus 로고    scopus 로고
    • β-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike
    • Kreisberg J.F., Betts S.D., and King J. β-helix core packing within the triple-stranded oligomerization domain of the P22 tailspike. Protein Sci. 9 (2000) 2338-2343
    • (2000) Protein Sci. , vol.9 , pp. 2338-2343
    • Kreisberg, J.F.1    Betts, S.D.2    King, J.3
  • 35
    • 0036093824 scopus 로고    scopus 로고
    • Crystal structure of β-helical antifreeze protein points to a general ice binding model
    • Leinala E.K., Davies P.L., and Jia Z.C. Crystal structure of β-helical antifreeze protein points to a general ice binding model. Structure 10 (2002) 619-627
    • (2002) Structure , vol.10 , pp. 619-627
    • Leinala, E.K.1    Davies, P.L.2    Jia, Z.C.3
  • 36
    • 0034691568 scopus 로고    scopus 로고
    • Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein
    • Liou Y.C., Tocilj A., Davies P.L., and Jia Z.C. Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein. Nature 406 (2000) 322-324
    • (2000) Nature , vol.406 , pp. 322-324
    • Liou, Y.C.1    Tocilj, A.2    Davies, P.L.3    Jia, Z.C.4
  • 39
    • 0036081257 scopus 로고    scopus 로고
    • Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant
    • Massi F., Klimov D., Thirumalai D., and Straub J.E. Charge states rather than propensity for β-structure determine enhanced fibrillogenesis in wild-type Alzheimer's β-amyloid peptide compared to E22Q Dutch mutant. Protein Sci. 11 (2002) 1639-1647
    • (2002) Protein Sci. , vol.11 , pp. 1639-1647
    • Massi, F.1    Klimov, D.2    Thirumalai, D.3    Straub, J.E.4
  • 40
    • 0036414287 scopus 로고    scopus 로고
    • Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide
    • Mazor Y., Gilead S., Benhar I., and Gazit E. Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide. J. Mol. Biol. 322 (2002) 1013-1024
    • (2002) J. Mol. Biol. , vol.322 , pp. 1013-1024
    • Mazor, Y.1    Gilead, S.2    Benhar, I.3    Gazit, E.4
  • 41
    • 0041519431 scopus 로고    scopus 로고
    • A new perspective on beta-sheet structures using vibrational Raman optical activity: from poly(L-lysine) to the prion protein
    • McColl L.H., Blanch E.W., Gill A.C., Rhie A.G.O., Ritchie M.A., Hecht L., Nielsen K., and Barron L.D. A new perspective on beta-sheet structures using vibrational Raman optical activity: from poly(L-lysine) to the prion protein. J. Am. Chem. Soc. 125 (2003) 10019-10026
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10019-10026
    • McColl, L.H.1    Blanch, E.W.2    Gill, A.C.3    Rhie, A.G.O.4    Ritchie, M.A.5    Hecht, L.6    Nielsen, K.7    Barron, L.D.8
  • 42
    • 0034710897 scopus 로고    scopus 로고
    • A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions
    • Michelitsch M.D., and Weissman J.S. A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions. Proc. Natl. Acad. Sci. USA 97 (2000) 11910-11915
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11910-11915
    • Michelitsch, M.D.1    Weissman, J.S.2
  • 45
    • 1642417648 scopus 로고    scopus 로고
    • Amyloid fibrils from the viewpoint of protein folding
    • Ohnishi S., and Takano K. Amyloid fibrils from the viewpoint of protein folding. Cell. Mol. Life Sci. 61 (2004) 511-524
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 511-524
    • Ohnishi, S.1    Takano, K.2
  • 48
    • 0037313696 scopus 로고    scopus 로고
    • A primordial structure underlying amyloid
    • Pickersgill R.W. A primordial structure underlying amyloid. Structure 11 (2003) 137-138
    • (2003) Structure , vol.11 , pp. 137-138
    • Pickersgill, R.W.1
  • 50
    • 0037466613 scopus 로고    scopus 로고
    • Casting metal nanowires within discrete self-assembled peptide nanotubes
    • Reches M., and Gazit E. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300 (2003) 625-627
    • (2003) Science , vol.300 , pp. 625-627
    • Reches, M.1    Gazit, E.2
  • 51
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson J.S., and Richardson D.C. Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl. Acad. Sci. USA 99 (2002) 2754-2759
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 52
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: themes and variations
    • Rochet J.C., and Lansbury P.T. Amyloid fibrillogenesis: themes and variations. Curr. Opin. Struct. Biol. 10 (2000) 60-68
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 60-68
    • Rochet, J.C.1    Lansbury, P.T.2
  • 53
    • 3543022080 scopus 로고    scopus 로고
    • Scrambled prion domains form prions and amyloid
    • Ross E.D., Baxa U., and Wickner R.B. Scrambled prion domains form prions and amyloid. Mol. Cell. Biol. 24 (2004) 7206-7213
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7206-7213
    • Ross, E.D.1    Baxa, U.2    Wickner, R.B.3
  • 55
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: structure and assembly
    • Serpell L.C. Alzheimer's amyloid fibrils: structure and assembly. Biochim. Biophys. Acta 1502 (2000) 16-30
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 56
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
    • Stefani M., and Dobson C.M. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 81 (2003) 678-699
    • (2003) J. Mol. Med. , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 58
    • 20444363123 scopus 로고    scopus 로고
    • Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: Significant role of Asn ladder
    • Tsai H.-H., Reches M., Gunasekaran K., Tsai C.-J., Gazit E., and Nussinov R. Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: Significant role of Asn ladder. Proc. Natl. Acad. Sci. USA 102 (2005) 8174-8179
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8174-8179
    • Tsai, H.-H.1    Reches, M.2    Gunasekaran, K.3    Tsai, C.-J.4    Gazit, E.5    Nussinov, R.6
  • 59
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko R. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14 (2004) 96-103
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 62
    • 0036052739 scopus 로고    scopus 로고
    • Ideas of order for amyloid fibril structure
    • Wetzel R. Ideas of order for amyloid fibril structure. Structure 10 (2002) 1031-1036
    • (2002) Structure , vol.10 , pp. 1031-1036
    • Wetzel, R.1
  • 64
    • 0029058159 scopus 로고
    • An analysis of side-chain interactions and pair correlations within antiparallel β-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters M.A., and Curmi P.M.G. An analysis of side-chain interactions and pair correlations within antiparallel β-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins 22 (1995) 119-131
    • (1995) Proteins , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.G.2
  • 65
    • 0035909921 scopus 로고    scopus 로고
    • The free energy landscape for β-hairpin folding in explicit water
    • Zhou R.H., Berne B.J., and Germain R. The free energy landscape for β-hairpin folding in explicit water. Proc. Natl. Acad. Sci. USA 98 (2001) 14931-14936
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14931-14936
    • Zhou, R.H.1    Berne, B.J.2    Germain, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.