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Volumn 38, Issue 2, 2012, Pages 139-143

Molecular dynamics simulation of intrinsically disordered proteins

Author keywords

intrinsically disordered proteins; molecular dynamics; tau protein

Indexed keywords

3D STRUCTURE; AVERAGE VALUES; DISORDERED PROTEINS; DYNAMICAL SIMULATION; GYRATION RADII; MOLECULAR DYNAMICS SIMULATIONS; PRIMARY SEQUENCES; PROTEIN DATA BANK; SOLVENT MOLECULES; TAU PROTEINS;

EID: 84856279313     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927022.2011.608671     Document Type: Article
Times cited : (14)

References (17)
  • 1
    • 84856303283 scopus 로고    scopus 로고
    • Intrinsically disordered proteins
    • J. Sussman, and I. Silman, eds., World Scientific, Singapore
    • P. Tompa, Intrinsically disordered proteins, in Structural Proteomics and its Impact on the Life Sciences, J. Sussman, and I. Silman, eds., World Scientific, Singapore, 2008, pp. 153-180.
    • (2008) Structural Proteomics and its Impact on the Life Sciences , pp. 153-180
    • Tompa, P.1
  • 4
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • P. Tompa, Intrinsically Unstructured Proteins, Trends Biochem. Sci. 27 (2002), pp. 527-533. (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 5
    • 52949123661 scopus 로고    scopus 로고
    • Domain conformation of tau protein studied by solution small-angle X-ray scattering
    • E. Mylonas, A. Hascher, P. Bernadò, M. Blackledge, E. Mandelkow, and D.I. Svergun, Domain Conformation of Tau Protein Studied by Solution Small-Angle X-ray Scattering, Biochemistry 47 (2008), pp. 10345-10353.
    • (2008) Biochemistry , vol.47 , pp. 10345-10353
    • Mylonas, E.1    Hascher, A.2    Bernadò, P.3    Blackledge, M.4    Mandelkow, E.5    Svergun, D.I.6
  • 6
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • DOI 10.1016/j.febslet.2005.03.072, PII S0014579305004242
    • P. Tompa, The interplay between structure and function in intrinsically unstructured proteins, FEBS Lett. 579 (2005), pp. 3346-3354. (Pubitemid 40804685)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3346-3354
    • Tompa, P.1
  • 8
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • DOI 10.1152/physrev.00024.2003
    • J. Avila, J.J. Lucas, M. Pérez, and F. Hernàndez, Role of Tau Protein in Both Physiological and Pathological Conditions, Physiol. Rev. 84 (2004), pp. 361-384. (Pubitemid 38365487)
    • (2004) Physiological Reviews , vol.84 , Issue.2 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 14
    • 0344778061 scopus 로고
    • Semianalytical treatment of solvation for molecular mechanics and dynamics
    • C. Still, A. Tempczyk, R.C. Hawley, and T. Hendrickson, Semianalytical Treatment of Solvation for Molecular Mechanics and Dynamics, J. Am. Chem. Soc. 112 (1990), pp. 6127-6129.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 6127-6129
    • Still, C.1    Tempczyk, A.2    Hawley, R.C.3    Hendrickson, T.4
  • 15
    • 33847723384 scopus 로고    scopus 로고
    • Secondary structure bias in generalized born solvent models: Comparison of conformational ensembles and free energy of solvent polarization from explicit and implicit solvation
    • DOI 10.1021/jp066831u
    • D.R. Roe, A. Okur, L. Wickstrom, V. Hornak, and C. Simmerling, Secondary Structure Bias in Generalized Born Solvent Models: Comparison of Conformational Ensembles and Free Energy of Solvent Polarization from Explicit and Implicit Solvation, J. Phys. Chem. B 111 (2007), pp. 1846-1857. (Pubitemid 46384278)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.7 , pp. 1846-1857
    • Roe, D.R.1    Okur, A.2    Wickstrom, L.3    Hornak, V.4    Simmerling, C.5
  • 16
    • 33749603363 scopus 로고    scopus 로고
    • How well does Poisson-Boltzmann implicit solvent agree with explicit solvent? A quantitative analysis
    • DOI 10.1021/jp063479b
    • C. Tan, L. Yang, and R. Luo, How Well Does Poisson-Boltzmann Implicit Solvent Agree with Explicit Solvent? A Quantitative Analysis, J. Phys. Chem. B 110 (2006), pp. 18680-18687. (Pubitemid 44547378)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.37 , pp. 18680-18687
    • Tan, C.1    Yang, L.2    Luo, R.3
  • 17
    • 0035497783 scopus 로고    scopus 로고
    • Proteins in vacuo: Denaturing and folding mechanisms studied with computersimulated molecular dynamics
    • G.A. Arteca, C.T. Reimann, and O. Tapia, Proteins in vacuo: Denaturing and folding mechanisms studied with computersimulated molecular dynamics, Mass Spectrosc. Rev. 20 (2001), pp. 402-422.
    • (2001) Mass Spectrosc. Rev. , vol.20 , pp. 402-422
    • Arteca, G.A.1    Reimann, C.T.2    Tapia, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.