메뉴 건너뛰기




Volumn 10, Issue SUPPL. 1, 2009, Pages

Studying the unfolding process of protein G and protein L under physical property space

Author keywords

[No Author keywords available]

Indexed keywords

CARTESIAN COORDINATE; CARTESIAN SPACE; NATIVE STATE; PROPERTY SPACES; PROTEIN FOLDING MECHANISMS; PROTEIN G; SIMULATION TIME; UNFOLDING PROCESS;

EID: 60849110265     PISSN: None     EISSN: 14712105     Source Type: Journal    
DOI: 10.1186/1471-2105-10-S1-S44     Document Type: Article
Times cited : (6)

References (27)
  • 1
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • 10.1038/35011000 10811210
    • Baker D A surprising simplicity to protein folding Nature 2000, 405:39-42 10.1038/35011000 10811210
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 2
    • 0033117763 scopus 로고    scopus 로고
    • Matching theory and experiment in protein folding
    • 10.1016/S0959-440X(99)80027-X 10322214
    • Alm E Baker D Matching theory and experiment in protein folding Curr Opin Struct Biol 1999, 9:189-196 10.1016/S0959-440X(99)80027-X 10322214
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 189-196
    • Alm, E.1    Baker, D.2
  • 4
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved
    • 10.1038/14896 10542091
    • Martinez JC Serrano L The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved Nature Struct Biol 1999, 6:1010-1016 10.1038/14896 10542091
    • (1999) Nature Struct Biol , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 5
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • 10.1006/jmbi.1998.1645 9545386
    • Plaxco KW Simons KT Baker D Contact order, transition state placement and the refolding rates of single domain proteins J Mol Biol 1998, 277:985-994 10.1006/jmbi.1998.1645 9545386
    • (1998) J Mol Biol , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 6
    • 0042510944 scopus 로고    scopus 로고
    • Contact order revisited: Influence of protein size on the folding rate
    • 2324001 12931003 10.1110/ps.0302503
    • Ivankov DN Garbuzynskiy SO Alm E Plaxco KW Baker D Finkelstein AV Contact order revisited: Influence of protein size on the folding rate Protein Sci 2003, 12(9):2057-62 2324001 12931003 10.1110/ps.0302503
    • (2003) Protein Sci , vol.12 , Issue.9 , pp. 2057-2062
    • Ivankov, D.N.1    Garbuzynskiy, S.O.2    Alm, E.3    Plaxco, K.W.4    Baker, D.5    Finkelstein, A.V.6
  • 7
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of β-hairpin formation in protein G folding
    • 10.1038/77971 10932252
    • McCallister EL Alm E Baker D Critical role of β-hairpin formation in protein G folding Nat Struct Biol 2000, 7:669-673 10.1038/77971 10932252
    • (2000) Nat Struct Biol , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 8
    • 0036785556 scopus 로고    scopus 로고
    • The origins of asymmetry in the folding transition states of protein L and protein G
    • 2373711 12237457 10.1110/ps.0205402
    • Karanicolas J Brooks CLIII The origins of asymmetry in the folding transition states of protein L and protein G Protein Sci 2002, 11:2351-2361 2373711 12237457 10.1110/ps.0205402
    • (2002) Protein Sci , vol.11 , pp. 2351-2361
    • Karanicolas, J.1    Brooks, C.L.I.I.I.2
  • 9
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • 10.1006/jmbi.2000.3701 10801362
    • Kim DE Fisher C Baker D A breakdown of symmetry in the folding transition state of protein L J Mol Biol 2000, 298:971-984 10.1006/ jmbi.2000.3701 10801362
    • (2000) J Mol Biol , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 10
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "on-route" intermediates for protein folding? An investigation for small globular proteins
    • 10.1006/jmbi.2000.3693 10801360
    • Cecilla C Nelson O Topological and energetic factors: What determines the structural details of the transition state ensemble and "on-route" intermediates for protein folding? An investigation for small globular proteins J Mol Biol 2000, 298:937-953 10.1006/ jmbi.2000.3693 10801360
    • (2000) J Mol Biol , vol.298 , pp. 937-953
    • Cecilla, C.1    Nelson, O.2
  • 11
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein-folding mechanism from free-energy landscape derived from native structures
    • 18029 10500172 10.1073/pnas.96.20.11305
    • Alm E Baker D Prediction of protein-folding mechanism from free-energy landscape derived from native structures PNAS 1999, 96:11305-11310 18029 10500172 10.1073/pnas.96.20.11305
    • (1999) PNAS , vol.96 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 12
    • 44049094482 scopus 로고    scopus 로고
    • Study of Multiple Unfolding Trajectories and Unfolded States of the Protein GB1 Under the Physical Property Space
    • 18399694
    • Ji-Hua W Li-Ling Z Xiang-Hua D Study of Multiple Unfolding Trajectories and Unfolded States of the Protein GB1 Under the Physical Property Space J Biomol Struct Dyn 2008, 25:609-620 18399694
    • (2008) J Biomol Struct Dyn , vol.25 , pp. 609-620
    • Ji-Hua, W.1    Li-Ling, Z.2    Xiang-Hua, D.3
  • 13
    • 0025769350 scopus 로고
    • A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G
    • 10.1126/science.1871600 1871600
    • Gronenborn AM Filpula DR Essig NZ Achari A Whitlow M Wingfield PT Clore GM A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G Science 1991, 253:657-661 10.1126/ science.1871600 1871600
    • (1991) Science , vol.253 , pp. 657-661
    • Gronenborn, A.M.1    Filpula, D.R.2    Essig, N.Z.3    Achari, A.4    Whitlow, M.5    Wingfield, P.T.6    Clore, G.M.7
  • 14
    • 0027155337 scopus 로고
    • Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L
    • 10.1021/bi00064a023 8461301
    • Wikstrom M Sjobring U Kastern W Bjorck L Drakenberg T Forsen S Proton nuclear magnetic resonance sequential assignments and secondary structure of an immunoglobulin light chain-binding domain of protein L Biochemistry 1993, 32:3381-3386 10.1021/bi00064a023 8461301
    • (1993) Biochemistry , vol.32 , pp. 3381-3386
    • Wikstrom, M.1    Sjobring, U.2    Kastern, W.3    Bjorck, L.4    Drakenberg, T.5    Forsen, S.6
  • 15
    • 0028109545 scopus 로고
    • Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G
    • 10.1021/bi00251a008 7947810
    • Wikstrom M Drakenberg T Forsen S Sjobring U Bjorck L Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G Biochemistry 1994, 33:14011-14017 10.1021/bi00251a008 7947810
    • (1994) Biochemistry , vol.33 , pp. 14011-14017
    • Wikstrom, M.1    Drakenberg, T.2    Forsen, S.3    Sjobring, U.4    Bjorck, L.5
  • 16
    • 0032080053 scopus 로고    scopus 로고
    • Calculations on folding of segment B1 of streptococcal protein G
    • 10.1006/jmbi.1998.1688 9571063
    • Sheinerman FB Brooks CL Calculations on folding of segment B1 of streptococcal protein G J Mol Biol 1998, 278:439-456 10.1006/ jmbi.1998.1688 9571063
    • (1998) J Mol Biol , vol.278 , pp. 439-456
    • Sheinerman, F.B.1    Brooks, C.L.2
  • 17
    • 0031465967 scopus 로고    scopus 로고
    • "New view" of protein folding reconciled with the old through multiple unfolding simulations
    • 10.1126/science.278.5345.1928 9395391
    • Lazaridis T Karplus M "New view" of protein folding reconciled with the old through multiple unfolding simulations Science 1997, 278:1928-1931 10.1126/science.278.5345.1928 9395391
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 18
    • 0026782853 scopus 로고
    • Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G
    • 10.1021/bi00147a006 1510916
    • Alexander P Orban J Bryan P Kinetic analysis of folding and unfolding the 56 amino acid IgG-binding domain of streptococcal protein G Biochemistry 1992, 31:7243-7248 10.1021/bi00147a006 1510916
    • (1992) Biochemistry , vol.31 , pp. 7243-7248
    • Alexander, P.1    Orban, J.2    Bryan, P.3
  • 19
    • 0030900533 scopus 로고    scopus 로고
    • Kinetics of folding of the IgG binding domain of peptostreptococcal protein L
    • 10.1021/bi9625758 9116017
    • Scalley ML Yi Q Gu H McCormack A Yates JR Baker D Kinetics of folding of the IgG binding domain of peptostreptococcal protein L Biochemistry 1997, 36(11):3373-3382 10.1021/bi9625758 9116017
    • (1997) Biochemistry , vol.36 , Issue.11 , pp. 3373-3382
    • Scalley, M.L.1    Yi, Q.2    Gu, H.3    McCormack, A.4    Yates, J.R.5    Baker, D.6
  • 20
    • 0036215854 scopus 로고    scopus 로고
    • Folding rate prediction using total contact distance
    • 1302485 11751332 10.1016/S0006-3495(02)75410-6
    • Hongyi Z Yaoqi Z Folding rate prediction using total contact distance Biophys J 2002, 82:458-463 1302485 11751332 10.1016/S0006-3495(02)75410-6
    • (2002) Biophys J , vol.82 , pp. 458-463
    • Hongyi, Z.1    Yaoqi, Z.2
  • 21
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules
    • 10.1006/jmbi.1997.1148 9245603
    • Plaxco KW Spitzfaden C Campbell ID Dobson CM A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules J Mol Biol 1997, 270:763-770 10.1006/jmbi.1997.1148 9245603
    • (1997) J Mol Biol , vol.270 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 22
    • 0032584783 scopus 로고    scopus 로고
    • Reversible peptide folding in solution by molecular dynamics simulation
    • 10.1006/jmbi.1998.1885 9671560
    • Daura X Jaun B Seebach D van Gunsteren WF Mark AE Reversible peptide folding in solution by molecular dynamics simulation J Mol Biol 1998, 280:925-932 10.1006/jmbi.1998.1885 9671560
    • (1998) J Mol Biol , vol.280 , pp. 925-932
    • Daura, X.1    Jaun, B.2    Seebach, D.3    van Gunsteren, W.F.4    Mark, A.E.5
  • 24
    • 0033557181 scopus 로고    scopus 로고
    • Folding-unfolding thermodynamics of a β-heptapeptide from equilibrium simulations
    • 10.1002/(SICI)1097-0134(19990215)34:3<269::AID-PROT1>3.0.CO;2-3 10024015
    • Daura X van Gunsteren WF Mark AE Folding-unfolding thermodynamics of a β-heptapeptide from equilibrium simulations Proteins Struct Funct Genet 1999, 34:269-280 10.1002/ (SICI)1097-0134(19990215)34:3<269::AID-PROT1>3.0.CO;2-3 10024015
    • (1999) Proteins Struct Funct Genet , vol.34 , pp. 269-280
    • Daura, X.1    van Gunsteren, W.F.2    Mark, A.E.3
  • 27
    • 1242346370 scopus 로고
    • The missing term in effective pair potentials
    • 10.1021/j100308a038
    • Berendsen HJC Grigera JR Straatsma TP The missing term in effective pair potentials J Phys Chem 1987, 91:6269-6271 10.1021/j100308a038
    • (1987) J Phys Chem , vol.91 , pp. 6269-6271
    • Berendsen, H.J.C.1    Grigera, J.R.2    Straatsma, T.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.