메뉴 건너뛰기




Volumn 64, Issue 1-3, 1997, Pages 45-57

Local fluctuations and global unfolding of partially folded BPTI detected by NMR

Author keywords

Chemical exchange; Equilibrium thermodynamics; NMR; Protein folding; Segmental motions

Indexed keywords

APROTININ;

EID: 0030939174     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(96)02210-7     Document Type: Conference Paper
Times cited : (18)

References (23)
  • 1
    • 0029145759 scopus 로고
    • Dynamic structure of a highly ordered β-sheet molten globule: Multiple conformations with a stable core
    • E. Barbar, G. Barany and C. Woodward, Dynamic structure of a highly ordered β-sheet molten globule: Multiple conformations with a stable core, Biochemistry, 34 (1995) 11423-11434.
    • (1995) Biochemistry , vol.34 , pp. 11423-11434
    • Barbar, E.1    Barany, G.2    Woodward, C.3
  • 2
    • 0028966372 scopus 로고
    • Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor
    • M. Ferrer, G. Barany and C. Woodward, Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor, Nature Struct. Biol., 2 (1995) 211-218.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 211-218
    • Ferrer, M.1    Barany, G.2    Woodward, C.3
  • 3
    • 0028805413 scopus 로고
    • Extensive non-random structure in reduced and unfolded bovine pan-creatic trypsin inhibitor
    • H. Pan, E. Barbar, G. Barany and C. Woodward, Extensive non-random structure in reduced and unfolded bovine pan-creatic trypsin inhibitor, Biochemistry, 34 (1995) 13974-13981.
    • (1995) Biochemistry , vol.34 , pp. 13974-13981
    • Pan, H.1    Barbar, E.2    Barany, G.3    Woodward, C.4
  • 4
    • 0343807273 scopus 로고
    • Detection of a third native one-disulfide intermediate in the folding of BPTI
    • M. Dadlez and P. Kim, Detection of a third native one-disulfide intermediate in the folding of BPTI, Nature Struct. Biol., 2 (1995) 6-12.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 6-12
    • Dadlez, M.1    Kim, P.2
  • 5
    • 0030342680 scopus 로고    scopus 로고
    • Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink
    • E. Barbar, G. Barany and C. Woodward, Unfolded BPTI variants with a single disulfide bond have diminished non-native structure distant from the crosslink, Folding and Design 1 (1996) 65-76.
    • (1996) Folding and Design , vol.1 , pp. 65-76
    • Barbar, E.1    Barany, G.2    Woodward, C.3
  • 6
    • 0001817424 scopus 로고    scopus 로고
    • Optimized methods for chemical synthesis of bovine pancreatic trypsin inhibitor analogues
    • (Marshak, D., ed) Academic Press, San Diego
    • G. Barany, C.M. Gross, M. Ferrer, E. Barbar, H. Pan and C. Woodward, Optimized methods for chemical synthesis of bovine pancreatic trypsin inhibitor analogues, Techniques in Protein Chemistry VII, (Marshak, D., ed) Academic Press, San Diego, 1996, pp. 503-514.
    • (1996) Techniques in Protein Chemistry VII , pp. 503-514
    • Barany, G.1    Gross, C.M.2    Ferrer, M.3    Barbar, E.4    Pan, H.5    Woodward, C.6
  • 8
    • 0000195671 scopus 로고
    • Natural abundance Nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • G. Bodenhausen and D. Ruben, Natural abundance Nitrogen-15 NMR by enhanced heteronuclear spectroscopy, Chem. Phys. Lett., 69 (1980) 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.2
  • 9
    • 48749147783 scopus 로고
    • An improved sequence for broadband decoupling: WALTZ-16
    • A. J. Shaka, J. Keeler, T. Frenkiel and R. Freeman, An improved sequence for broadband decoupling: WALTZ-16, J. Magn. Reson., 52 (1983) 335-338.
    • (1983) J. Magn. Reson. , vol.52 , pp. 335-338
    • Shaka, A.J.1    Keeler, J.2    Frenkiel, T.3    Freeman, R.4
  • 10
    • 32544454854 scopus 로고
    • Calibration of the methanol and glycol nuclear magnetic resonance thermometers with a static thermistor probe
    • A.L. Van Geet, Calibration of the methanol and glycol nuclear magnetic resonance thermometers with a static thermistor probe, Anal. Chem., 40 (1968) 2227-2229.
    • (1968) Anal. Chem. , vol.40 , pp. 2227-2229
    • Van Geet, A.L.1
  • 11
  • 12
    • 0028673096 scopus 로고
    • Analysis of multidimensional spectroscopic data to monitor unfolding of proteins
    • M.R. Eftink and G.D. Ramsay, Analysis of multidimensional spectroscopic data to monitor unfolding of proteins, Methods Enzymol., 240 (1994) 615-645.
    • (1994) Methods Enzymol. , vol.240 , pp. 615-645
    • Eftink, M.R.1    Ramsay, G.D.2
  • 13
    • 0004978084 scopus 로고
    • Academic Press, New York
    • J. Sandström, in Dynamic NMR, Academic Press, New York, 1982.
    • (1982) Dynamic NMR
    • Sandström, J.1
  • 14
    • 0017394828 scopus 로고
    • Cis-trans equilibrium and kinetic studies of acetyl-L-proline and glycyl-L-proline
    • H.N. Cheng and F.A. Bovey, Cis-trans equilibrium and kinetic studies of acetyl-L-proline and glycyl-L-proline, Biopolymers, 16 (1977) 1465-1472.
    • (1977) Biopolymers , vol.16 , pp. 1465-1472
    • Cheng, H.N.1    Bovey, F.A.2
  • 16
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • K.A. Dill and D. Shortle, Denatured states of proteins, Annu. Rev. Biochem., 60 (1991) 795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 17
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigation of nearest-neighbor effects, J. Biomol. NMR, 5 (1995) 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 18
    • 0029036496 scopus 로고
    • Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer
    • O. Zhang and J. Forman-Kay, Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer, Biochemistry, 34 (1995) 6784-6794.
    • (1995) Biochemistry , vol.34 , pp. 6784-6794
    • Zhang, O.1    Forman-Kay, J.2
  • 19
    • 0030580089 scopus 로고    scopus 로고
    • Structure based calculation of the equilibrium folding pathway of proteins. Correlations with hydrogen exchange protection factors
    • V. Hilser and E. Freire, Structure based calculation of the equilibrium folding pathway of proteins. Correlations with hydrogen exchange protection factors, J. Mol. Biol., 262 (1996) 756-772.
    • (1996) J. Mol. Biol. , vol.262 , pp. 756-772
    • Hilser, V.1    Freire, E.2
  • 20
    • 0019872611 scopus 로고
    • Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea
    • B. Hilton, K. Trudeau and C. Woodward, Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea, Biochemistry, 20 (1981) 4697-4703.
    • (1981) Biochemistry , vol.20 , pp. 4697-4703
    • Hilton, B.1    Trudeau, K.2    Woodward, C.3
  • 21
    • 0027504749 scopus 로고
    • Hydrogen exchange identifies native-state motional domains important in protein folding
    • K.-S. Kim, J. Fuchs and C. Woodward, Hydrogen exchange identifies native-state motional domains important in protein folding, Biochemistry, 32 (1993), 9600-9608.
    • (1993) Biochemistry , vol.32 , pp. 9600-9608
    • Kim, K.-S.1    Fuchs, J.2    Woodward, C.3
  • 22
    • 0027375522 scopus 로고
    • Internal flexibility and global stability of proteins: Effect of urea on hydrogen exchange rates of BPTI
    • K.-S. Kim and C. Woodward, Internal flexibility and global stability of proteins: Effect of urea on hydrogen exchange rates of BPTI, Biochemistry, 32 (1993), 9609-9613.
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.-S.1    Woodward, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.