메뉴 건너뛰기




Volumn 8, Issue 5, 2013, Pages

Variation in Structure of a Protein (H2AX) with Knowledge-Based Interactions

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2AX;

EID: 84878533344     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0064507     Document Type: Article
Times cited : (10)

References (17)
  • 1
    • 0017021957 scopus 로고
    • Medium and long range interaction parameters between amino acids for predicting three dimensional structures of proteins
    • Tanaka S, Scheraga HA, (1976) Medium and long range interaction parameters between amino acids for predicting three dimensional structures of proteins. Macromolecules 9: 945-950.
    • (1976) Macromolecules , vol.9 , pp. 945-950
    • Tanaka, S.1    Scheraga, H.A.2
  • 2
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation
    • Miyazawa S, Jernigan RL, (1985) Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation. Macromolecules 18: 534-552.
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 3
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term for simulation and treading
    • Miyazawa S, Jernigan RL, (1996) Residue-residue potentials with a favorable contact pair term for simulation and treading. J Mol Biol 256: 623-644.
    • (1996) J Mol Biol , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 4
    • 84878602573 scopus 로고    scopus 로고
    • Web site for residue-residue interaction tables:, courtesy of the research group of R.L. Jernigan
    • Web site for residue-residue interaction tables: http://gor.bb.iastate.edu/potential/, courtesy of the research group of R.L. Jernigan.
  • 5
    • 0041319042 scopus 로고    scopus 로고
    • The Origin and Extent of Coarse Grained Irregularities in Protein Internal Packing I
    • Bagci Z, Kloczkowski A, Jernigan RL, Bahar I, (2003) The Origin and Extent of Coarse Grained Irregularities in Protein Internal Packing I. Proteins. 53: 56-67.
    • (2003) Proteins , vol.53 , pp. 56-67
    • Bagci, Z.1    Kloczkowski, A.2    Jernigan, R.L.3    Bahar, I.4
  • 6
    • 0027524668 scopus 로고
    • Calculation of protein backbone geometry from alpha-carbon coordinates based on peptide-group dipole alignment
    • Liwo A, Pincus MR, Wawak RJ, Rackovsky S, Scheraga HA, (1993) Calculation of protein backbone geometry from alpha-carbon coordinates based on peptide-group dipole alignment. Prot Sci 2: 1697-1714.
    • (1993) Prot Sci , vol.2 , pp. 1697-1714
    • Liwo, A.1    Pincus, M.R.2    Wawak, R.J.3    Rackovsky, S.4    Scheraga, H.A.5
  • 7
    • 0033005899 scopus 로고    scopus 로고
    • Pair potentials for protein folding: choice of reference states and sensitivity of predicted native states to variations in the interaction schemes
    • Betancourt MR, Thirumalai D, (1999) Pair potentials for protein folding: choice of reference states and sensitivity of predicted native states to variations in the interaction schemes. Protein Sci 2: 361-369.
    • (1999) Protein Sci , vol.2 , pp. 361-369
    • Betancourt, M.R.1    Thirumalai, D.2
  • 8
    • 0035427382 scopus 로고    scopus 로고
    • How to guarantee optimal stability for most representative structures in the protein data bank
    • Bastolla U, Farwer J, Knapp EW, Vendruscolo M, (2001) How to guarantee optimal stability for most representative structures in the protein data bank. Proteins 44: 79-96.
    • (2001) Proteins , vol.44 , pp. 79-96
    • Bastolla, U.1    Farwer, J.2    Knapp, E.W.3    Vendruscolo, M.4
  • 9
    • 0026785519 scopus 로고
    • Contact potential that recognizes the correct folding of globular proteins
    • Maiorov VN, Crippen GM, (1992) Contact potential that recognizes the correct folding of globular proteins. J Mol Biol 227: 876-888.
    • (1992) J Mol Biol , vol.227 , pp. 876-888
    • Maiorov, V.N.1    Crippen, G.M.2
  • 10
    • 0030584681 scopus 로고    scopus 로고
    • Knowledge-based potentials for protein folding: what can we learn from protein structures?
    • Godzik A, Kolinski A, Skolnick J, (1996) Knowledge-based potentials for protein folding: what can we learn from protein structures? Proteins 4: 363-366.
    • (1996) Proteins , vol.4 , pp. 363-366
    • Godzik, A.1    Kolinski, A.2    Skolnick, J.3
  • 11
    • 0030983768 scopus 로고    scopus 로고
    • Derivation and testing of pair potentials for protein folding: When is the quasichemical approximation correct?
    • Skolnick J, Jaroszewski L, Kolinski A, (1997) Derivation and testing of pair potentials for protein folding: When is the quasichemical approximation correct? Protein Sci 6: 676-688.
    • (1997) Protein Sci , vol.6 , pp. 676-688
    • Skolnick, J.1    Jaroszewski, L.2    Kolinski, A.3
  • 12
    • 84858597132 scopus 로고    scopus 로고
    • Conformational temperature-dependent behavior of a histone h2ax: A coarse-grained Monte Carlo approach via knowledge-based interaction potentials
    • (and the references therein)
    • Fritsche M, Pandey RB, Farmer BL, Heermann D (2012) Conformational temperature-dependent behavior of a histone h2ax: A coarse-grained Monte Carlo approach via knowledge-based interaction potentials. PLoS one 7: e32075-1- e32075-8. (and the references therein).
    • (2012) PLoS one , vol.7 , pp. 1-8
    • Fritsche, M.1    Pandey, R.B.2    Farmer, B.L.3    Heermann, D.4
  • 13
    • 84869133970 scopus 로고    scopus 로고
    • Random coil to globular thermal response of a protein (H3.1) with three knowledge-based coarse-grained potentials
    • Pandey RB, Farmer BL (2012) Random coil to globular thermal response of a protein (H3.1) with three knowledge-based coarse-grained potentials. PLoS one 7: e49352-1- e32075-9.
    • (2012) PLoS one , vol.7 , pp. 1-9
    • Pandey, R.B.1    Farmer, B.L.2
  • 14
    • 77957572546 scopus 로고    scopus 로고
    • Challenges in protein-folding simulations, Nature Physics
    • Freddolino PL, Harrison CB, Liu Y, Schulten K, (2010) Challenges in protein-folding simulations, Nature Physics. 6: 751-758.
    • (2010) , vol.6 , pp. 751-758
    • Freddolino, P.L.1    Harrison, C.B.2    Liu, Y.3    Schulten, K.4
  • 15
    • 85040099247 scopus 로고    scopus 로고
    • Monte Carlo Simulation in Statistical Physics
    • Fifth edition
    • Binder K, Heermann DW, (2010) Monte Carlo Simulation in Statistical Physics Springer Fifth edition.
    • (2010) Springer
    • Binder, K.1    Heermann, D.W.2
  • 16
    • 77956444309 scopus 로고    scopus 로고
    • Bio-functionalization and immobilization of a membrane via peptide binding (CR3-1, S2) by a Monte Carlo simulation
    • Pandey RB, Heinz H, Feng J, Farmer BL, (2010) Bio-functionalization and immobilization of a membrane via peptide binding (CR3-1, S2) by a Monte Carlo simulation. J. Chem. Phys. 133: 095102-095108.
    • (2010) J. Chem. Phys , vol.133 , pp. 095102-095108
    • Pandey, R.B.1    Heinz, H.2    Feng, J.3    Farmer, B.L.4
  • 17
    • 62349101755 scopus 로고    scopus 로고
    • Adsorption of peptides (A3, Flg, Pd2, Pd4) on gold and palladium surfaces by a coarse-grained Monte Carlo simulation
    • Pandey RB, Heinz H, Feng J, Farmer BL, Slocik JM, et al. (2009) Adsorption of peptides (A3, Flg, Pd2, Pd4) on gold and palladium surfaces by a coarse-grained Monte Carlo simulation, Phys. Chem. Chem. Phys. 11: 1989-2001.
    • (2009) Phys. Chem. Chem. Phys , vol.11 , pp. 1989-2001
    • Pandey, R.B.1    Heinz, H.2    Feng, J.3    Farmer, B.L.4    Slocik, J.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.