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Volumn 18, Issue 2, 2004, Pages 203-211

Single molecule force spectroscopy studies of DNA denaturation by T4 gene 32 protein

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOMEDICAL ENGINEERING; DNA; FREE ENERGY; MELTING; NUCLEIC ACIDS; PROTEINS;

EID: 2442665172     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2004/403203     Document Type: Conference Paper
Times cited : (21)

References (45)
  • 1
    • 0034530126 scopus 로고    scopus 로고
    • Single molecule force spectroscopy in biology using the atomic force microscope
    • J. Zlatanova, S.M. Lindsay and S.H. Leuba, Single molecule force spectroscopy in biology using the atomic force microscope, Progr. Biophys. Molec. Biol. 74 (2000), 37-61.
    • (2000) Progr. Biophys. Molec. Biol. , vol.74 , pp. 37-61
    • Zlatanova, J.1    Lindsay, S.M.2    Leuba, S.H.3
  • 2
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • S.B. Smith, Y.J. Cui and C. Bustamante, Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules, Science 271 (1996), 795-799.
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.J.2    Bustamante, C.3
  • 3
    • 0026495432 scopus 로고
    • Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads
    • S.B. Smith, L. Finzi and C. Bustamante, Direct mechanical measurements of the elasticity of single DNA molecules by using magnetic beads, Science 258 (1992), 1122-1126.
    • (1992) Science , vol.258 , pp. 1122-1126
    • Smith, S.B.1    Finzi, L.2    Bustamante, C.3
  • 4
    • 0034710990 scopus 로고    scopus 로고
    • Replication by a single DNA polymerase of a stretched single-stranded DNA
    • B. Maier, D. Bensimon and V. Croquette, Replication by a single DNA polymerase of a stretched single-stranded DNA, Proc. Nat. Acad. Sci. USA 97 (2000), 12002-12007.
    • (2000) Proc. Nat. Acad. Sci. USA , vol.97 , pp. 12002-12007
    • Maier, B.1    Bensimon, D.2    Croquette, V.3
  • 6
    • 0037832291 scopus 로고    scopus 로고
    • Stretching DNA and RNA to probe their interactions with proteins
    • J.F. Allemand, D. Bensimon and V. Croquette, Stretching DNA and RNA to probe their interactions with proteins, Curr. Opin. Struct. Biol. 13 (2003), 266-274.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 266-274
    • Allemand, J.F.1    Bensimon, D.2    Croquette, V.3
  • 7
    • 0036600949 scopus 로고    scopus 로고
    • Force spectroscopy of single DNA and RNA molecules
    • M.C. Williams and I. Rouzina, Force spectroscopy of single DNA and RNA molecules, Curr. Opin. Struct. Biol. 12 (2002), 330-336.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 330-336
    • Williams, M.C.1    Rouzina, I.2
  • 8
    • 0035144565 scopus 로고    scopus 로고
    • The effect of pH on the overstretching transition of dsDNA: Evidence of force-induced DNA melting
    • M.C. Williams, J.R. Wenner, I. Rouzina and V.A. Bloomfield, The effect of pH on the overstretching transition of dsDNA: Evidence of force-induced DNA melting, Biophys. J. 80 (2001), 874-881.
    • (2001) Biophys. J. , vol.80 , pp. 874-881
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 9
    • 0035072057 scopus 로고    scopus 로고
    • Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching
    • M.C. Williams, J.R. Wenner, I. Rouzina and V.A. Bloomfield, Entropy and heat capacity of DNA melting from temperature dependence of single molecule stretching, Biophys. J. 80 (2001), 1932-1939.
    • (2001) Biophys. J. , vol.80 , pp. 1932-1939
    • Williams, M.C.1    Wenner, J.R.2    Rouzina, I.3    Bloomfield, V.A.4
  • 11
    • 0037173118 scopus 로고    scopus 로고
    • Specific zinc finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function
    • M.C. Williams, R.J. Gorelick and K. Musier-Forsyth, Specific zinc finger architecture required for HIV-1 nucleocapsid protein's nucleic acid chaperone function, Proc. Nat. Acad. Sci. USA 99 (2002), 8614-8619.
    • (2002) Proc. Nat. Acad. Sci. USA , vol.99 , pp. 8614-8619
    • Williams, M.C.1    Gorelick, R.J.2    Musier-Forsyth, K.3
  • 12
    • 0344406718 scopus 로고    scopus 로고
    • Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains
    • K. Pant, R.L. Karpel and M.C. Williams, Kinetic regulation of single DNA molecule denaturation by T4 gene 32 protein structural domains, J. Molec. Biol. 327 (2003), 571-578.
    • (2003) J. Molec. Biol. , vol.327 , pp. 571-578
    • Pant, K.1    Karpel, R.L.2    Williams, M.C.3
  • 14
    • 0029909230 scopus 로고    scopus 로고
    • Molecular dynamics simulation of DNA stretching is consistent with the tension observed for extension and strand separation and predicts a novel ladder structure
    • M.W. Konrad and J.I. Bolonick, Molecular dynamics simulation of DNA stretching is consistent with the tension observed for extension and strand separation and predicts a novel ladder structure, J. Am. Chem. Soc. 118 (1996), 10989-10994.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10989-10994
    • Konrad, M.W.1    Bolonick, J.I.2
  • 15
    • 0029899989 scopus 로고    scopus 로고
    • Modelling extreme stretching of DNA
    • A. Lebrun and R. Lavery, Modelling extreme stretching of DNA, Nucleic Acids Res. 24 (1996), 2260-2267.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2260-2267
    • Lebrun, A.1    Lavery, R.2
  • 17
    • 34548455815 scopus 로고
    • Nucleic acid: An extensible molecule?
    • M.H.F. Wilkins, R.G. Gosling and W.E. Seeds, Nucleic acid: an extensible molecule? Nature 167 (1951), 759-760.
    • (1951) Nature , vol.167 , pp. 759-760
    • Wilkins, M.H.F.1    Gosling, R.G.2    Seeds, W.E.3
  • 18
    • 0035146646 scopus 로고    scopus 로고
    • Force-induced melting of the DNA double helix. 1. Thermodynamic analysis
    • I. Rouzina and V.A. Bloomfield, Force-induced melting of the DNA double helix. 1. Thermodynamic analysis, Biophys. J. 80 (2001), 882-893.
    • (2001) Biophys. J. , vol.80 , pp. 882-893
    • Rouzina, I.1    Bloomfield, V.A.2
  • 19
    • 0035144566 scopus 로고    scopus 로고
    • Force-induced melting of the DNA double helix. 2. Effect of solution conditions
    • I. Rouzina and V.A. Bloomfield, Force-induced melting of the DNA double helix. 2. Effect of solution conditions, Biophys. J. 80 (2001), 894-900.
    • (2001) Biophys. J. , vol.80 , pp. 894-900
    • Rouzina, I.1    Bloomfield, V.A.2
  • 20
    • 0036009140 scopus 로고    scopus 로고
    • Thermodynamics of DNA interactions from single molecule stretching experiments
    • M.C. Williams, I. Rouzina and V.A. Bloomfield, Thermodynamics of DNA interactions from single molecule stretching experiments, Accounts Chem. Res. 35 (2002), 159-166.
    • (2002) Accounts Chem. Res. , vol.35 , pp. 159-166
    • Williams, M.C.1    Rouzina, I.2    Bloomfield, V.A.3
  • 23
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • E. Evans and K. Ritchie, Dynamic strength of molecular adhesion bonds, Biophys. J. 72 (1997), 1541-1555.
    • (1997) Biophys. J. , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 24
    • 0036106380 scopus 로고    scopus 로고
    • Salt dependence of the elasticity and overstretching transition of single DNA molecules
    • J.R. Wenner, M.C. Williams, I. Rouzina and V.A. Bloomfield, Salt dependence of the elasticity and overstretching transition of single DNA molecules, Biophys. J. 82 (2002), 3160-3169.
    • (2002) Biophys. J. , vol.82 , pp. 3160-3169
    • Wenner, J.R.1    Williams, M.C.2    Rouzina, I.3    Bloomfield, V.A.4
  • 27
    • 0035333546 scopus 로고    scopus 로고
    • Structural transitions in DNA driven by external force and torque
    • A. Sarkar, J.-F. Léger, D. Chatenay and J.F. Marko, Structural transitions in DNA driven by external force and torque, Phys. Rev. E 63 (2001), 051903.
    • (2001) Phys. Rev. E , vol.63 , pp. 051903
    • Sarkar, A.1    Léger, J.-F.2    Chatenay, D.3    Marko, J.F.4
  • 29
    • 0033405042 scopus 로고    scopus 로고
    • Transport of torsional stress in DNA
    • P. Nelson, Transport of torsional stress in DNA, Proc. Nat. Acad. Sci. USA 96 (1999), 14342-14347.
    • (1999) Proc. Nat. Acad. Sci. USA , vol.96 , pp. 14342-14347
    • Nelson, P.1
  • 32
    • 85015087906 scopus 로고    scopus 로고
    • Ten years of tension: Single-molecule DNA mechanics
    • C. Bustamante, Z. Bryant and S.B. Smith, Ten years of tension: single-molecule DNA mechanics, Nature 421 (2003), 423-427.
    • (2003) Nature , vol.421 , pp. 423-427
    • Bustamante, C.1    Bryant, Z.2    Smith, S.B.3
  • 35
    • 0036015495 scopus 로고    scopus 로고
    • A distinctive single-strand DNA-binding protein from the Archaeon Sulfolobus solfataricus
    • C.A. Haseltine and S.C. Kowalczykoski, A distinctive single-strand DNA-binding protein from the Archaeon Sulfolobus solfataricus, Mol. Microbiol. 43 (2002), 1505-1515.
    • (2002) Mol. Microbiol. , vol.43 , pp. 1505-1515
    • Haseltine, C.A.1    Kowalczykoski, S.C.2
  • 36
    • 0036314935 scopus 로고    scopus 로고
    • Biochemical properties of single-stranded DNA-binding protein from Mycobacterium smegmatis, a fast-growing mycobacterium and its physical and functional interaction with uracil DNA glycosylases
    • N. Acharya and U. Varshney, Biochemical properties of single-stranded DNA-binding protein from Mycobacterium smegmatis, a fast-growing mycobacterium and its physical and functional interaction with uracil DNA glycosylases, J. Mol. Biol. 318 (2002), 1251-1264.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1251-1264
    • Acharya, N.1    Varshney, U.2
  • 37
    • 0029052511 scopus 로고
    • Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA
    • Y. Shamoo, A.M. Friedman, M.R. Parsons, W.H. Konigsberg and T.A. Steitz, Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA, Nature 376 (1995), 362-366.
    • (1995) Nature , vol.376 , pp. 362-366
    • Shamoo, Y.1    Friedman, A.M.2    Parsons, M.R.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 38
    • 0033525654 scopus 로고    scopus 로고
    • Details of the nucleic acid binding site of T4 gene 32 protein revealed by proteolysis and DNA Tm depression methods
    • M. Wu, E.K. Flynn and R.L. Karpel, Details of the nucleic acid binding site of T4 gene 32 protein revealed by proteolysis and DNA Tm depression methods, J. Mol. Biol. 286 (1999), 1107-1121.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1107-1121
    • Wu, M.1    Flynn, E.K.2    Karpel, R.L.3
  • 39
    • 0016302387 scopus 로고
    • Denaturation of T4 DNA by an in vitro processed gene 32-protein
    • J. Hosoda, B. Takacs and C. Brack, Denaturation of T4 DNA by an in vitro processed gene 32-protein, FEBS Lett. 47 (1974), 338-342.
    • (1974) FEBS Lett. , vol.47 , pp. 338-342
    • Hosoda, J.1    Takacs, B.2    Brack, C.3
  • 40
    • 0035951867 scopus 로고    scopus 로고
    • Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein
    • L. Waidner, E. Flynn, M. Wu, X. Li and R.L. Karpel, Domain effects on the DNA-interactive properties of bacteriophage T4 gene 32 protein, J. Biol. Chem. 276 (2001), 2509-2516.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2509-2516
    • Waidner, L.1    Flynn, E.2    Wu, M.3    Li, X.4    Karpel, R.L.5
  • 41
    • 0017145254 scopus 로고
    • DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures
    • D.E. Jensen, R.C. Kelly and P.H. von Hippel, DNA "melting" proteins. II. Effects of bacteriophage T4 gene 32-protein binding on the conformation and stability of nucleic acid structures, J. Biol. Chem. 251 (1976), 7215-7228.
    • (1976) J. Biol. Chem. , vol.251 , pp. 7215-7228
    • Jensen, D.E.1    Kelly, R.C.2    Von Hippel, P.H.3
  • 43
    • 0019350732 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32P*III)
    • N. Lonberg, S.C. Kowalczykowski, L.S. Paul and P.H. von Hippel, Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. III. Binding properties of two specific proteolytic digestion products of the protein (G32P*I and G32P*III), J. Mol. Biol. 145 (1981), 123-138.
    • (1981) J. Mol. Biol. , vol.145 , pp. 123-138
    • Lonberg, N.1    Kowalczykowski, S.C.2    Paul, L.S.3    Von Hippel, P.H.4
  • 44
    • 33751156715 scopus 로고
    • Stiff chains and filaments under tension
    • T. Odijk, Stiff chains and filaments under tension, Macromolecules 28 (1995), 7016-7018.
    • (1995) Macromolecules , vol.28 , pp. 7016-7018
    • Odijk, T.1
  • 45
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis, MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures, J. App. Crystallogr. 24 (1991), 946-950.
    • (1991) J. App. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.