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Volumn 298, Issue , 2012, Pages 77-81

Sonication-induced unfolding proteins

Author keywords

Diagnostic ultrasound; Probability; Protein; Stability

Indexed keywords

ACOUSTICS; BIOPHYSICS; PROBABILITY; PROTEIN; STOCHASTICITY; VIBRATION;

EID: 84857292397     PISSN: 00225193     EISSN: 10958541     Source Type: Journal    
DOI: 10.1016/j.jtbi.2012.01.008     Document Type: Article
Times cited : (5)

References (33)
  • 2
    • 0034697986 scopus 로고    scopus 로고
    • What can disulphide bonds tell us about protein energetic, function and folding: simulations and bioinformatics analysis
    • Abkevich V.I., Shakhnovich E.I. What can disulphide bonds tell us about protein energetic, function and folding: simulations and bioinformatics analysis. J. Mol. Biol. 2000, 300:975-985.
    • (2000) J. Mol. Biol. , vol.300 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 4
    • 0037160126 scopus 로고    scopus 로고
    • Kinetic intermediate in the folding of human prion protein
    • Apetri A., Surevicz W.K. Kinetic intermediate in the folding of human prion protein. J. Biol. Chem. 2002, 27(7):44589-44592.
    • (2002) J. Biol. Chem. , vol.27 , Issue.7 , pp. 44589-44592
    • Apetri, A.1    Surevicz, W.K.2
  • 6
    • 0034905392 scopus 로고    scopus 로고
    • Intracranial temperature elevation from diagnostic ultrasound
    • Barnett S.B. Intracranial temperature elevation from diagnostic ultrasound. Ultrasound Med. Biol. 2000, 27(7):883-888.
    • (2000) Ultrasound Med. Biol. , vol.27 , Issue.7 , pp. 883-888
    • Barnett, S.B.1
  • 7
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins?
    • Barth A., Zscherp C. What vibrations tell us about proteins?. Q. Rev. Biophys. 2002, 35(4):369-430.
    • (2002) Q. Rev. Biophys. , vol.35 , Issue.4 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 10
    • 0020730848 scopus 로고
    • Low-frequency vibrations of helical structures in protein molecules
    • Chou K.C. Low-frequency vibrations of helical structures in protein molecules. Biochem. J 1983, 209:573-580.
    • (1983) Biochem. J , vol.209 , pp. 573-580
    • Chou, K.C.1
  • 11
    • 0021188468 scopus 로고
    • The biological functions of low-frequency vibrations (phonons). Resonance effects and allosteric transition
    • Chou K.C. The biological functions of low-frequency vibrations (phonons). Resonance effects and allosteric transition. Biophys. Chem. 1984, 20:61-71.
    • (1984) Biophys. Chem. , vol.20 , pp. 61-71
    • Chou, K.C.1
  • 12
    • 56249088601 scopus 로고    scopus 로고
    • Hazard, risks, and safety of diagnostic ultrasound
    • Duck F.A. Hazard, risks, and safety of diagnostic ultrasound. Med. Eng. Phys. 2008, 30:1338-1348.
    • (2008) Med. Eng. Phys. , vol.30 , pp. 1338-1348
    • Duck, F.A.1
  • 18
    • 33645960997 scopus 로고    scopus 로고
    • Protein stability and dynamics in the pressure-temperature plane
    • Meersman, F., Smeller, L., Heremans, K., 2006. Protein stability and dynamics in the pressure-temperature plane. Biochim. Biophys. Acta 1764, 346-354.
    • (2006) Biochim. Biophys. Acta , pp. 346-354
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 19
    • 70349232202 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding dynamics at the secondary structure level
    • Mukherjee S., Waegele M.M., Chowdhury P., Guo L., Gai F. Effects of macromolecular crowding on protein folding dynamics at the secondary structure level. J. Mol. Biol. 2009, 393:227-236.
    • (2009) J. Mol. Biol. , vol.393 , pp. 227-236
    • Mukherjee, S.1    Waegele, M.M.2    Chowdhury, P.3    Guo, L.4    Gai, F.5
  • 20
    • 0009969074 scopus 로고
    • Structure energetics of protein stability and folding cooperativity
    • Murphy K.P., Preire E. Structure energetics of protein stability and folding cooperativity. Pure Appl. Chem. 1993, 65(9):1939-1946.
    • (1993) Pure Appl. Chem. , vol.65 , Issue.9 , pp. 1939-1946
    • Murphy, K.P.1    Preire, E.2
  • 21
    • 0035003478 scopus 로고    scopus 로고
    • Biological effects of ultrasound: development of safety guidelines. Part II: General review
    • Nyborg W.L. Biological effects of ultrasound: development of safety guidelines. Part II: General review. Ultrasound Med. Biol. 2001, 27(3):301-333.
    • (2001) Ultrasound Med. Biol. , vol.27 , Issue.3 , pp. 301-333
    • Nyborg, W.L.1
  • 24
    • 20144369761 scopus 로고    scopus 로고
    • Stability of proteins: temperature, pressure and the role of the solvent
    • Scharmagl C., Reif M., Friedrich J. Stability of proteins: temperature, pressure and the role of the solvent. Biochim. Biophys. Acta 2005, 1749:187-213.
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 187-213
    • Scharmagl, C.1    Reif, M.2    Friedrich, J.3
  • 25
    • 0034743155 scopus 로고    scopus 로고
    • From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding
    • Shea J.E., Brooks C.I. From folding theories to folding proteins: a review and assessment of simulation studies of protein folding and unfolding. Annu. Rev. Cell Dev. Biol. 2001, 52:499-535.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.52 , pp. 499-535
    • Shea, J.E.1    Brooks, C.I.2
  • 26
    • 33645019704 scopus 로고    scopus 로고
    • An enhanced elastic network model to represent the motions of domain-swapped proteins
    • Song G., Jernigan R.L. An enhanced elastic network model to represent the motions of domain-swapped proteins. Proteins:Struct., Funct., Bioinf. 2006, 63:197-209.
    • (2006) Proteins:Struct., Funct., Bioinf. , vol.63 , pp. 197-209
    • Song, G.1    Jernigan, R.L.2
  • 27
    • 22144469126 scopus 로고    scopus 로고
    • Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study
    • Spencer D.S., Xu K., Logan T.M., Zhou H. Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study. J. Mol. Biol. 2005, 351:219-232.
    • (2005) J. Mol. Biol. , vol.351 , pp. 219-232
    • Spencer, D.S.1    Xu, K.2    Logan, T.M.3    Zhou, H.4
  • 29
    • 84857345241 scopus 로고
    • VCH Publishers Inc, New York, K.S. Suslick (Ed.)
    • 1988, VCH Publishers Inc, New York. K.S. Suslick (Ed.).
    • (1988)
  • 30
    • 2942567954 scopus 로고    scopus 로고
    • Describing protein folding kinetics by molecular dynamics simulations.1.Theory
    • Swope W.C., Pitera J.W. Describing protein folding kinetics by molecular dynamics simulations.1.Theory. J. Phys. Chem. B 2004, 108:6571-6581.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 6571-6581
    • Swope, W.C.1    Pitera, J.W.2
  • 31
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton J.M. Disulphide bridges in globular proteins. J. Mol. Biol. 1981, 151:261-287.
    • (1981) J. Mol. Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 32
    • 84857345243 scopus 로고    scopus 로고
    • World Scientific Publishing Co, J. Wu, W.L.M. Nyborg (Eds.)
    • 2006, World Scientific Publishing Co. J. Wu, W.L.M. Nyborg (Eds.).
    • (2006)
  • 33
    • 0242606993 scopus 로고    scopus 로고
    • Modeling free energy of a rigid protein in solid water: comparison between rigid-body motions and harmonic oscillators
    • Yoshioki S. Modeling free energy of a rigid protein in solid water: comparison between rigid-body motions and harmonic oscillators. Physica A 2004, 331:552-570.
    • (2004) Physica A , vol.331 , pp. 552-570
    • Yoshioki, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.