메뉴 건너뛰기




Volumn 2006, Issue , 2006, Pages

Temperature-dependent loop formation kinetics in flexible peptides studied by time-resolved fluorescence spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords


EID: 33746883224     PISSN: 1110662X     EISSN: 1110662X     Source Type: Journal    
DOI: 10.1155/IJP/2006/89638     Document Type: Article
Times cited : (11)

References (38)
  • 3
    • 0037186549 scopus 로고    scopus 로고
    • Structure and dynamics of KH domains from FBP bound to single-stranded DNA
    • clore@speck.niddk.nih.gov
    • D. T. Braddock J. M. Louis J. L. Baber D. Levens G. M. Clore clore@speck.niddk.nih.gov Structure and dynamics of KH domains from FBP bound to single-stranded DNA. Nature 415 2002 6875 1051 1056
    • (2002) Nature , vol.415 , Issue.6875 , pp. 1051-1056
    • Braddock, D.T.1    Louis, J.M.2    Baber, J.L.3    Levens, D.4    Clore, G.M.5
  • 4
    • 0035967884 scopus 로고    scopus 로고
    • Modulation of antigenicity related to changes in antibody flexibility upon lyophilization
    • N. Taschner S. A. Müller V. R. Alumella Modulation of antigenicity related to changes in antibody flexibility upon lyophilization. Journal of Molecular Biology 310 2001 1 169 179
    • (2001) Journal of Molecular Biology , vol.310 , Issue.1 , pp. 169-179
    • Taschner, N.1    Müller, S.A.2    Alumella, V.R.3
  • 6
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H. J. Dyson P. E. Wright Intrinsically unstructured proteins and their functions. Nature Reviews Molecular Cell Biology 6 2005 3 197 208
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 7
    • 0032506017 scopus 로고    scopus 로고
    • Limited internal friction in the rate-limiting step of a two-state protein folding reaction
    • baker@ben.bchem.washington.edu
    • K. W. Plaxco D. Baker baker@ben.bchem.washington.edu Limited internal friction in the rate-limiting step of a two-state protein folding reaction. Proceedings of the National Academy of Sciences of the United States of America 95 1998 23 13591 13596
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.23 , pp. 13591-13596
    • Plaxco, K.W.1    Baker, D.2
  • 10
    • 4744357562 scopus 로고    scopus 로고
    • Internal friction controls the speed of protein folding from a compact configuration
    • S. A. Pabit H. Roder S. J. Hagen Internal friction controls the speed of protein folding from a compact configuration. Biochemistry 43 2004 39 12532 12538
    • (2004) Biochemistry , vol.43 , Issue.39 , pp. 12532-12538
    • Pabit, S.A.1    Roder, H.2    Hagen, S.J.3
  • 11
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. evidence for a two-state transition
    • S. E. Jackson A. R. Fersht Folding of chymotrypsin inhibitor 2. 1. evidence for a two-state transition. Biochemistry 30 1991 43 10428 10435
    • (1991) Biochemistry , vol.30 , Issue.43 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 12
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • A. Ansari C. M. Jones E. R. Henry J. Hofrichter W. A. Eaton The role of solvent viscosity in the dynamics of protein conformational changes. Science 256 1992 5065 1796 1798
    • (1992) Science , vol.256 , Issue.5065 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 13
    • 0035793222 scopus 로고    scopus 로고
    • Rate of intrachain contact formation in an unfolded protein: Temperature and denaturant effects
    • sjhagen@ufl.edu
    • S. J. Hagen sjhagen@ufl.edu C. W. Carswell E. M. Sjolander Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects. Journal of Molecular Biology 305 2001 5 1161 1171
    • (2001) Journal of Molecular Biology , vol.305 , Issue.5 , pp. 1161-1171
    • Hagen, S.J.1    Carswell, C.W.2    Sjolander, E.M.3
  • 14
    • 0001931668 scopus 로고
    • Unfolded proteins, compact states and molten globules
    • C. M. Dobson Unfolded proteins, compact states and molten globules. Current Opinion in Structural Biology 2 1992 1 6 12
    • (1992) Current Opinion in Structural Biology , vol.2 , Issue.1 , pp. 6-12
    • Dobson, C.M.1
  • 15
    • 0033532201 scopus 로고    scopus 로고
    • Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
    • doniach@drizzle.stanford.edu kiefhaber@ubaclu.unibas.ch
    • D. J. Segel A. Bachmann J. Hofrichter K. O. Hodgson S. Doniach doniach@drizzle.stanford.edu T. Kiefhaber kiefhaber@ubaclu.unibas.ch Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. Journal of Molecular Biology 288 1999 3 489 499
    • (1999) Journal of Molecular Biology , vol.288 , Issue.3 , pp. 489-499
    • Segel, D.J.1    Bachmann, A.2    Hofrichter, J.3    Hodgson, K.O.4    Doniach, S.5    Kiefhaber, T.6
  • 18
    • 14944346760 scopus 로고    scopus 로고
    • Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains
    • F. Krieger A. Möglich T. Kiefhaber Effect of proline and glycine residues on dynamics and barriers of loop formation in polypeptide chains. Journal of the American Chemical Society 127 2005 10 3346 3352
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.10 , pp. 3346-3352
    • Krieger, F.1    Möglich, A.2    Kiefhaber, T.3
  • 20
    • 85037227289 scopus 로고    scopus 로고
    • Dynamics of intramolecular contact formation in polypeptides: Distance dependence of quenching rates in a room-temperature glass
    • L. J. Lapidus W. A. Eaton J. Hofrichter Dynamics of intramolecular contact formation in polypeptides: distance dependence of quenching rates in a room-temperature glass. Physical Review Letters 87 2001 25 258101/1 258101/4
    • (2001) Physical Review Letters , vol.87 , Issue.25
    • Lapidus, L.J.1    Eaton, W.A.2    Hofrichter, J.3
  • 21
    • 0037196288 scopus 로고    scopus 로고
    • A fluorescence-based method for direct measurement of submicrosecond intramolecular contact formation in biopolymers: An exploratory study with polypeptides
    • R. R. Hudgins F. Huang G. Gramlich W. M. Nau A fluorescence-based method for direct measurement of submicrosecond intramolecular contact formation in biopolymers: an exploratory study with polypeptides. Journal of the American Chemical Society 124 2002 4 556 564
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.4 , pp. 556-564
    • Hudgins, R.R.1    Huang, F.2    Gramlich, G.3    Nau, W.M.4
  • 22
    • 0038319135 scopus 로고    scopus 로고
    • A conformational flexibility scale for amino acids in peptides
    • F. Huang W. M. Nau A conformational flexibility scale for amino acids in peptides. Angewandte Chemie International Edition 42 2003 20 2269 2272
    • (2003) Angewandte Chemie International Edition , vol.42 , Issue.20 , pp. 2269-2272
    • Huang, F.1    Nau, W.M.2
  • 23
    • 11444265452 scopus 로고    scopus 로고
    • Primary and secondary structure dependence of peptide flexibility assessed by fluorescence-based measurement of end-to-end collision rates
    • F. Huang R. R. Hudgins W. M. Nau Primary and secondary structure dependence of peptide flexibility assessed by fluorescence-based measurement of end-to-end collision rates. Journal of the American Chemical Society 126 2004 50 16665 16675
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.50 , pp. 16665-16675
    • Huang, F.1    Hudgins, R.R.2    Nau, W.M.3
  • 24
    • 25444492050 scopus 로고    scopus 로고
    • Photochemical techniques for studying the flexibility of polypeptides
    • F. Huang W. M. Nau Photochemical techniques for studying the flexibility of polypeptides. Research on Chemical Intermediates 31 2005 7-8 717 726
    • (2005) Research on Chemical Intermediates , vol.31 , Issue.7-8 , pp. 717-726
    • Huang, F.1    Nau, W.M.2
  • 25
    • 33646807480 scopus 로고    scopus 로고
    • Nanosecond time-resolved fluorescence protease assays
    • A. Hennig D. Roth T. Enderle W. M. Nau Nanosecond time-resolved fluorescence protease assays. ChemBioChem 7 2006 5 733 737
    • (2006) ChemBioChem , vol.7 , Issue.5 , pp. 733-737
    • Hennig, A.1    Roth, D.2    Enderle, T.3    Nau, W.M.4
  • 28
    • 13444282649 scopus 로고    scopus 로고
    • Refractive index effects on the oscillator strength and radiative decay rate of 2,3-diazabicyclo[2.2.2]oct-2-ene
    • J. Mohanty W. M. Nau Refractive index effects on the oscillator strength and radiative decay rate of 2,3-diazabicyclo[2.2.2]oct-2-ene. Photochemical and Photobiological Sciences 3 2004 11-12 1026 1031
    • (2004) Photochemical and Photobiological Sciences , vol.3 , Issue.11-12 , pp. 1026-1031
    • Mohanty, J.1    Nau, W.M.2
  • 29
    • 0001542628 scopus 로고    scopus 로고
    • Discrimination between hydrogen atom and proton abstraction in the quenching of
    • n,π* singlet-excited states by protic solvents
    • W. M. Nau G. Greiner H. Rau M. Olivucci M. A. Robb Discrimination between hydrogen atom and proton abstraction in the quenching of n,π* singlet-excited states by protic solvents. Berichte der Bunsen-Gesellschaft für Physikalische Chemie 102 1998 3 486 492
    • (1998) Berichte der Bunsen-Gesellschaft für Physikalische Chemie , vol.102 , Issue.3 , pp. 486-492
    • Nau, W.M.1    Greiner, G.2    Rau, H.3    Olivucci, M.4    Robb, M.A.5
  • 30
    • 0000630956 scopus 로고    scopus 로고
    • Fluorescence of 2,3-diazabicyclo[2.2.2]oct-2-ene revisited: Solvent-induced quenching of the
    • n,π*-excited state by an aborted hydrogen atom transfer
    • W. M. Nau G. Greiner H. Rau J. Wall M. Olivucci C. Scaiano Fluorescence of 2,3-diazabicyclo[2.2.2]oct-2-ene revisited: solvent-induced quenching of the n,π*-excited state by an aborted hydrogen atom transfer. Journal of Physical Chemistry A 103 1999 11 1579 1584
    • (1999) Journal of Physical Chemistry a , vol.103 , Issue.11 , pp. 1579-1584
    • Nau, W.M.1    Greiner, G.2    Rau, H.3    Wall, J.4    Olivucci, M.5    Scaiano, C.6
  • 32
    • 1642576003 scopus 로고    scopus 로고
    • Kinetics of end-to-end collision in short single-stranded nucleic acids
    • X. J. Wang W. M. Nau Kinetics of end-to-end collision in short single-stranded nucleic acids. Journal of the American Chemical Society 126 2004 3 808 813
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.3 , pp. 808-813
    • Wang, X.J.1    Nau, W.M.2
  • 33
    • 0344254793 scopus 로고    scopus 로고
    • Fluorescence quenching kinetics in short polymer chains: Dependence on chain length
    • X. Wang E. N. Bodunov W. M. Nau Fluorescence quenching kinetics in short polymer chains: dependence on chain length. Optics and Spectroscopy 95 2003 4 560 570
    • (2003) Optics and Spectroscopy , vol.95 , Issue.4 , pp. 560-570
    • Wang, X.1    Bodunov, E.N.2    Nau, W.M.3
  • 34
    • 0028941444 scopus 로고
    • Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor
    • C. J. Camacho D. Thirumalai Theoretical predictions of folding pathways by using the proximity rule, with applications to bovine pancreatic trypsin inhibitor. Proceedings of the National Academy of Sciences of the United States of America 92 1995 5 1277 1281
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.5 , pp. 1277-1281
    • Camacho, C.J.1    Thirumalai, D.2
  • 35
    • 0037067120 scopus 로고    scopus 로고
    • Peptide loop-closure kinetics from microsecond molecular dynamics simulations in explicit solvent
    • I.-C. Yeh G. Hummer Peptide loop-closure kinetics from microsecond molecular dynamics simulations in explicit solvent. Journal of the American Chemical Society 124 2002 23 6563 6568
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.23 , pp. 6563-6568
    • Yeh, I.-C.1    Hummer, G.2
  • 36
    • 34547925924 scopus 로고    scopus 로고
    • Kinetics of interior loop formation in semiflexible chains
    • C. Hyeon D. Thirumalai Kinetics of interior loop formation in semiflexible chains. Journal of Chemical Physics 124 2006 10 14 pages
    • (2006) Journal of Chemical Physics , vol.124 , Issue.10 , pp. 14
    • Hyeon, C.1    Thirumalai, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.