메뉴 건너뛰기




Volumn 134, Issue 17, 2011, Pages

Communication: The electrostatic polarization is essential to differentiate the helical propensity in polyalanine mutants

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROSTATIC POLARIZATION; EXPERIMENTAL MEASUREMENTS; FOLDING PROCESS; FORCE FIELDS; HELICAL CONTENT; HELIX FORMATION; MOLECULAR DYNAMICS SIMULATIONS; POLARIZATION EFFECT; POLYALANINE; POLYALANINE PEPTIDES; QUANTITATIVE DESCRIPTION; SEQUENCE VARIATIONS; TRIFLUOROETHANOL;

EID: 79957510489     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3581888     Document Type: Article
Times cited : (21)

References (38)
  • 1
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • DOI 10.1016/S0968-0004(99)01445-0, PII S0968000499014450
    • C. M. Dobson, Trends Biochem. Sci. 24, 329 (1999). 10.1016/S0968-0004(99) 01445-0 (Pubitemid 29421804)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 329-332
    • Dobson, C.M.1
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • F. Chiti and C. M. Dobson, Annu. Rev. Biochem. 75, 333 (2006). 10.1146/annurev.biochem.75.101304.123901 (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 4
    • 0037154980 scopus 로고    scopus 로고
    • Protein folding and unfolding at atomic resolution
    • DOI 10.1016/S0092-8674(02)00620-7
    • A. R. Fersht and V. Daggett, Cell 108, 573 (2002). 10.1016/S0092-8674(02) 00620-7 (Pubitemid 34260881)
    • (2002) Cell , vol.108 , Issue.4 , pp. 573-582
    • Fersht, A.R.1    Daggett, V.2
  • 5
    • 0034743155 scopus 로고    scopus 로고
    • From folding theories to folding proteins: A review and assessment of simulation studies of protein folding and unfolding
    • DOI 10.1146/annurev.physchem.52.1.499
    • J. E. Shea and C. L. Brooks III, Annu. Rev. Phys. Chem. 52, 499 (2001). 10.1146/annurev.physchem.52.1.499 (Pubitemid 33655131)
    • (2001) Annual Review of Physical Chemistry , vol.52 , pp. 499-535
    • Shea, J.-E.1    Brooks III, C.L.2
  • 11
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • DOI 10.1021/ja9621760, PII S0002786396021762
    • W. L. Jorgensen, D. S. Maxwell, and J. Tirado-Rives, J. Am. Chem. Soc. 118, 11225 (1996). 10.1021/ja9621760 (Pubitemid 26399746)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.45 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 13
    • 0242443693 scopus 로고    scopus 로고
    • Force fields for protein simulations
    • DOI 10.1016/S0065-3233(03)66002-X
    • J. W. Ponder and D. A. Case, Adv. Protein Chem. 66, 27 (2003). 10.1016/S0065-3233(03)66002-X (Pubitemid 37392314)
    • (2003) Advances in Protein Chemistry , vol.66 , pp. 27-85
    • Ponder, J.W.1    Case, D.A.2
  • 19
    • 51049101330 scopus 로고    scopus 로고
    • 10.1529/biophysj.108.131110
    • C. G. Ji, Y. Mei, and J. Z. H. Zhang, Biophys. J. 95, 1080 (2008). 10.1529/biophysj.108.131110
    • (2008) Biophys. J. , vol.95 , pp. 1080
    • Ji, C.G.1    Mei, Y.2    Zhang, J.Z.H.3
  • 20
    • 33748569544 scopus 로고    scopus 로고
    • A new quantum method for electrostatic solvation energy of protein
    • DOI 10.1063/1.2345201
    • Y. Mei, C. G. Ji, and J. Z. H. Zhang, J. Chem. Phys. 125, 94906 (2006). 10.1063/1.2345201 (Pubitemid 44370745)
    • (2006) Journal of Chemical Physics , vol.125 , Issue.9 , pp. 094906
    • Mei, Y.1    Ji, C.2    Zhang, J.Z.H.3
  • 28
    • 0026525048 scopus 로고
    • 10.1016/0022-2836(92)90264-K
    • V. Daggett and M. J. Levitt, J. Mol. Biol. 223, 1121 (1992). 10.1016/0022-2836(92)90264-K
    • (1992) J. Mol. Biol. , vol.223 , pp. 1121
    • Daggett, V.1    Levitt, M.J.2
  • 29
    • 0033181019 scopus 로고    scopus 로고
    • 10.1002/(SICI)1097-0134(19990801)36:2249::AID-PROT103.0.CO;2-1
    • S. Huo and J. E. Straub, Proteins: Struct. Funct. Genet. 36, 249 (1999). 10.1002/(SICI)1097-0134(19990801)36:2249::AID-PROT103.0.CO;2-1
    • (1999) Proteins: Struct. Funct. Genet. , vol.36 , pp. 249
    • Huo, S.1    Straub, J.E.2
  • 32
    • 25144490502 scopus 로고    scopus 로고
    • How large is an α-helix? Studies of the radii of gyration of helical peptides by small-angle X-ray scattering and molecular dynamics
    • DOI 10.1016/j.jmb.2005.08.053, PII S0022283605010077
    • B. Zagrovic, G. Jayachandran, I. S. Millett, S. Doniach, and V. S. Pande. J. Mol. Biol. 353, 232 (2005). 10.1016/j.jmb.2005.08.053 (Pubitemid 41356608)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 232-241
    • Zagrovic, B.1    Jayachandran, G.2    Millett, I.S.3    Doniach, S.4    Pande, V.S.5
  • 34
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • DOI 10.1006/jmbi.1994.1334
    • I. K. McDonald and J. M. Thornton, J. Mol. Biol. 238, 777 (1994). 10.1006/jmbi.1994.1334 (Pubitemid 24168633)
    • (1994) Journal of Molecular Biology , vol.238 , Issue.5 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 36
    • 79957521445 scopus 로고    scopus 로고
    • See supplementary material at E-JCPSA6-134-047116 for the simulation condition and comparison of partial atomic charges of AMBER and PPC for peptides Q, K, and D.
    • See supplementary material at http://dx.doi.org/10.1063/1.3581888 E-JCPSA6-134-047116 for the simulation condition and comparison of partial atomic charges of AMBER and PPC for peptides Q, K, and D.
  • 38
    • 33947475670 scopus 로고
    • 10.1021/bi00908a001
    • J. Hermans, Jr, Biochemistry 1, 193 (1962). 10.1021/bi00908a001
    • (1962) Biochemistry , vol.1 , pp. 193
    • Hermans Jr., J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.