메뉴 건너뛰기




Volumn 4, Issue 2, 1996, Pages 195-209

Structure and multiple conformations of the Kunitz-type domain from human type VI collagen α3(VI) chain in solution

Author keywords

Collagen; Kunitz type domain; NMR; Tertiary structure

Indexed keywords

BOVINAE;

EID: 0029644162     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00022-6     Document Type: Article
Times cited : (23)

References (60)
  • 1
    • 0025055088 scopus 로고
    • Mosaic structure of globular domains in the human type VI collagen α3 chain: Similarity to von Willebrand factor, fibronectin, actin, salivary proteins and aprotinin type protease inhibitors
    • Chu, M.-L., et al., & Timpl, R. (1990). Mosaic structure of globular domains in the human type VI collagen α3 chain: similarity to von Willebrand factor, fibronectin, actin, salivary proteins and aprotinin type protease inhibitors. EMBO J. 9, 385-393.
    • (1990) EMBO J. , vol.9 , pp. 385-393
    • Chu, M.-L.1    Timpl, R.2
  • 2
    • 0028072632 scopus 로고
    • Recombinant expression and properties of Kunitz-type protease inhibitor module from human type VI collagen α3(VI) chain
    • Mayer, U., et al., & Timpl, R. (1994). Recombinant expression and properties of Kunitz-type protease inhibitor module from human type VI collagen α3(VI) chain. Eur. J. Biochem. 225, 573-580.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 573-580
    • Mayer, U.1    Timpl, R.2
  • 3
    • 0023872043 scopus 로고
    • Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
    • Kitaguchi, N. Takahashi, Y., Tokushima, Y., Shiojiri, S. & Ito, H. (1988). Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity. Nature 331, 530-532.
    • (1988) Nature , vol.331 , pp. 530-532
    • Kitaguchi, N.1    Takahashi, Y.2    Tokushima, Y.3    Shiojiri, S.4    Ito, H.5
  • 4
    • 0023870043 scopus 로고
    • A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
    • Ponte, P., et al., & Cordell, B. (1988). A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature 331, 525-527.
    • (1988) Nature , vol.331 , pp. 525-527
    • Ponte, P.1    Cordell, B.2
  • 5
    • 0023850791 scopus 로고
    • Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease
    • Tanzi, R.E., McClatchey, A.I., Lamperti, E.D., Villa-Komaroff, L., Gusella, J.F. & Neve, R.-L (1988). Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease. Nature 331, 528-530.
    • (1988) Nature , vol.331 , pp. 528-530
    • Tanzi, R.E.1    McClatchey, A.I.2    Lamperti, E.D.3    Villa-Komaroff, L.4    Gusella, J.F.5    Neve, R.-L.6
  • 6
    • 0001612915 scopus 로고
    • Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution
    • Deisenhofer, J. & Steigemann, W. (1975). Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 Å resolution. Acta Cryst. B 31, 238-250.
    • (1975) Acta Cryst. B , vol.31 , pp. 238-250
    • Deisenhofer, J.1    Steigemann, W.2
  • 7
    • 0021603710 scopus 로고
    • Structure of bovine pancreatic trypsin inhibitor
    • Wlodawer, A., Walter, J., Huber, R. & Sjölin, L. (1984). Structure of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 180, 301-329.
    • (1984) J. Mol. Biol. , vol.180 , pp. 301-329
    • Wlodawer, A.1    Walter, J.2    Huber, R.3    Sjölin, L.4
  • 9
    • 0023120307 scopus 로고
    • Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor
    • Wlodawer, A., Deisenhofer, J. & Huber, R. (1987). Comparison of two highly refined structures of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 193, 145-156.
    • (1987) J. Mol. Biol. , vol.193 , pp. 145-156
    • Wlodawer, A.1    Deisenhofer, J.2    Huber, R.3
  • 10
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt, K.D., Güntert, P., Orbons, L.P.M. & Wüthrich, K. (1992). Determination of a high-quality nuclear magnetic resonance solution structure of bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol. Biol. 227, 757-775.
    • (1992) J. Mol. Biol. , vol.227 , pp. 757-775
    • Berndt, K.D.1    Güntert, P.2    Orbons, L.P.M.3    Wüthrich, K.4
  • 11
    • 0026511651 scopus 로고
    • Crystal structure of α-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor
    • Skarzynski, T. (1992). Crystal structure of α-dendrotoxin from the green mamba venom and its comparison with the structure of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 224, 671-683.
    • (1992) J. Mol. Biol. , vol.224 , pp. 671-683
    • Skarzynski, T.1
  • 12
    • 0025008384 scopus 로고
    • X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid β-protein precursor
    • Hynes, T.R., Randal, M., Kennedy, L.A., Eigenbrot, C. & Kossiakoff, A.A. (1990). X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid β-protein precursor. Biochemistry 29, 10018-10023.
    • (1990) Biochemistry , vol.29 , pp. 10018-10023
    • Hynes, T.R.1    Randal, M.2    Kennedy, L.A.3    Eigenbrot, C.4    Kossiakoff, A.A.5
  • 13
    • 0028982743 scopus 로고
    • 2-bungarotoxin. Potassium channel binding by Kunitz modules and targeted phospholipase action
    • 2-bungarotoxin. Potassium channel binding by Kunitz modules and targeted phospholipase action. Structure 3, 1109-1119.
    • (1995) Structure , vol.3 , pp. 1109-1119
    • Kwong, P.D.1    McDonald, N.Q.2    Sigler, P.B.3    Hendrickson, W.A.4
  • 14
    • 0027138664 scopus 로고
    • Nuclear magnetic resonance solution structure of dendrotoxin K from venom of Dendraoapsis polylepis polylepis
    • Berndt, K.D., Güntert, P. & Wüthrich, K. (1993). Nuclear magnetic resonance solution structure of dendrotoxin K from venom of Dendraoapsis polylepis polylepis. J. Mol. Biol. 234, 735-750.
    • (1993) J. Mol. Biol. , vol.234 , pp. 735-750
    • Berndt, K.D.1    Güntert, P.2    Wüthrich, K.3
  • 16
    • 0021095863 scopus 로고
    • Bovine pancreatic trypsin inhibitor has unusual thermodynamic stability parameters
    • Moses, E. & Hinz, H.-J. (1983). Bovine pancreatic trypsin inhibitor has unusual thermodynamic stability parameters. J. Mol. Biol. 170, 765-776.
    • (1983) J. Mol. Biol. , vol.170 , pp. 765-776
    • Moses, E.1    Hinz, H.-J.2
  • 17
    • 0023657725 scopus 로고
    • Stability studies on derivates of the bovine pancreatic trypsin inhibitor
    • Schwarz, H., Hinz, H.-J., Mehlich, A., Tschesche, H. & Wenzel, H.R. (1987). Stability studies on derivates of the bovine pancreatic trypsin inhibitor. Biochemistry 26, 3544-3551.
    • (1987) Biochemistry , vol.26 , pp. 3544-3551
    • Schwarz, H.1    Hinz, H.-J.2    Mehlich, A.3    Tschesche, H.4    Wenzel, H.R.5
  • 18
    • 0020475326 scopus 로고
    • 1H nuclear magnetic resonance spectra bovine pancreatic trypsin inhibitor
    • 1H nuclear magnetic resonance spectra bovine pancreatic trypsin inhibitor. J. Mol. Biol. 155, 347-366.
    • (1982) J. Mol. Biol. , vol.155 , pp. 347-366
    • Wagner, G.1    Wüthrich, K.2
  • 19
    • 0023645325 scopus 로고
    • Protein structures in solution by NMR and distance geometry. the polypeptide fold of the basic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Go, N. & Wüthrich, K. (1988). Protein structures in solution by NMR and distance geometry. The polypeptide fold of the basic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196, 611-639.
    • (1988) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 20
    • 0010467515 scopus 로고
    • 13C relaxation times and evidence for multiple conformations in the reactive site of BPTI
    • 13C relaxation times and evidence for multiple conformations in the reactive site of BPTI. Chem. Scripts 29A, 27-30.
    • (1989) Chem. Scripts , vol.29 A , pp. 27-30
    • Wagner, G.1    Nirmala, N.R.2
  • 21
    • 0027155345 scopus 로고
    • Disulfide bond isomerization in BPTI and BPTI(G36S): An NMR study of correlated mobility in proteins
    • Otting, G., Liepinsh, E. & Wüthrich, K. (1993). Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins. Biochemistry 32, 3571-3582.
    • (1993) Biochemistry , vol.32 , pp. 3571-3582
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 22
    • 0029108856 scopus 로고
    • The 1.6 Å structure of Kunitz-type domain from the α3 chain of human type VI collagen
    • Arnoux, et al., & Ducruix, A. (1995). The 1.6 Å structure of Kunitz-type domain from the α3 chain of human type VI collagen. J. Mol. Biol. 246, 609-617.
    • (1995) J. Mol. Biol. , vol.246 , pp. 609-617
    • Arnoux1    Ducruix, A.2
  • 24
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachman, P. & Ernst, R.R. (1979). Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachman, P.3    Ernst, R.R.4
  • 25
    • 84915716471 scopus 로고
    • Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura, S. & Ernst R.R. (1980). Elucidation of cross relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41, 95-117.
    • (1980) Mol. Phys. , vol.41 , pp. 95-117
    • Macura, S.1    Ernst, R.R.2
  • 26
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R.R. (1983). Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 27
    • 33845378943 scopus 로고
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy
    • 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J. Am. Chem. Soc. 107, 2820-2821.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2820-2821
    • Davis, D.G.1    Bax, A.2
  • 28
    • 0006393051 scopus 로고
    • Two dimensional spectroscopy: Application to nuclear magnetic resonance
    • Aue, W.P., Bartholdi, E. & Ernst, R.R. (1976). Two dimensional spectroscopy: application to nuclear magnetic resonance. J. Chem. Phys. 64, 2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 30
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-By, A.A., Stephens, R.L., Lee, J., Warren, C.D. & Jeanloz, R.W. (1984). Structure determination of a tetrasaccharide: transient nuclear Overhauser effects in the rotating frame. J. Am. Chem. Soc. 106, 811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-By, A.A.1    Stephens, R.L.2    Lee, J.3    Warren, C.D.4    Jeanloz, R.W.5
  • 31
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • Bax, A. & Davis, D.G. (1985). Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. A 63, 207-213.
    • (1985) J. Magn. Reson. A , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 32
    • 0021764802 scopus 로고
    • Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances
    • Wüthrich, K., Billeter, M. & Braun, W. (1984). Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. J. Mol. Biol. 180, 715-740.
    • (1984) J. Mol. Biol. , vol.180 , pp. 715-740
    • Wüthrich, K.1    Billeter, M.2    Braun, W.3
  • 33
    • 0023643824 scopus 로고
    • Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c
    • Hyberts, S.G., Mäki, W. & Wagner, G. (1987). Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin c. Eur. J. Biochem. 164, 625-635.
    • (1987) Eur. J. Biochem. , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Mäki, W.2    Wagner, G.3
  • 35
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D.S., Sykes, B.D. & F.M. Richards (1992). The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 36
    • 0000857486 scopus 로고
    • Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules
    • Otting, G. & Wüthrich, K. (1989). Studies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. J. Am. Chem. Soc. 111, 1871-1875.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 1871-1875
    • Otting, G.1    Wüthrich, K.2
  • 37
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W. & Huber, R. (1992). Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 38
    • 0024828095 scopus 로고
    • Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop
    • Holak, T.A., Bode, W., Huber, R., Otlewski, J. & Wilusz, T. (1989). Nuclear magnetic resonance solution and X-ray structures of squash trypsin inhibitor exhibit the same conformation of the proteinase binding loop. J. Mol. Biol. 210, 649-654.
    • (1989) J. Mol. Biol. , vol.210 , pp. 649-654
    • Holak, T.A.1    Bode, W.2    Huber, R.3    Otlewski, J.4    Wilusz, T.5
  • 39
    • 0024815191 scopus 로고
    • Determination of the complete 3-dimensional structure of the trypsin-inhibitor from squash seeds in aqueous-solution by nuclear magnetic-resonance and a combination of distance geometry and dynamical simulated annealing
    • Holak, T.A., Gondol, D., Otlewski, J. & Wilusz, T. (1989). Determination of the complete 3-dimensional structure of the trypsin-inhibitor from squash seeds in aqueous-solution by nuclear magnetic-resonance and a combination of distance geometry and dynamical simulated annealing. J. Mol. Biol. 210, 635-648.
    • (1989) J. Mol. Biol. , vol.210 , pp. 635-648
    • Holak, T.A.1    Gondol, D.2    Otlewski, J.3    Wilusz, T.4
  • 40
    • 0027944325 scopus 로고
    • Structure of leech derived tryptase inhibitor (LDT1-C) in solution
    • Mühlhahn, P., et al., & Holak, T.A. (1994). Structure of leech derived tryptase inhibitor (LDT1-C) in solution. FEBS Lett. 355, 290-296.
    • (1994) FEBS Lett. , vol.355 , pp. 290-296
    • Mühlhahn, P.1    Holak, T.A.2
  • 41
    • 0027092679 scopus 로고
    • The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures
    • Hyberts, S.G., Goldberg, M.S., Havel, T.F. & Wagner, G. (1992). The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X-ray structures. Protein Sci. 1, 736-751.40
    • (1992) Protein Sci. , vol.1
    • Hyberts, S.G.1    Goldberg, M.S.2    Havel, T.F.3    Wagner, G.4
  • 42
    • 0024846405 scopus 로고
    • Use of restrained molecular dynamics in water to determine three-dimensional protein structure: Prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II
    • Chiche., L., Gaboriaud, C., Heitz., A. Mornon, J.-P., Castro, B. & Kollman,P. A. (1989). Use of restrained molecular dynamics in water to determine three-dimensional protein structure: prediction of the three-dimensional structure of Ecballium elaterium trypsin inhibitor II. Proteins 6, 405-417.
    • (1989) Proteins , vol.6 , pp. 405-417
    • Chiche, L.1    Gaboriaud, C.2    Heitz, A.3    Mornon, J.-P.4    Castro, B.5    Kollman, P.A.6
  • 43
    • 0019333816 scopus 로고
    • On the nature of molecular conformations inferred from high-resolution NMR
    • Jardetzky, O. (1980). On the nature of molecular conformations inferred from high-resolution NMR. Biochem. Biophys. Acta 621, 227-232.
    • (1980) Biochem. Biophys. Acta , vol.621 , pp. 227-232
    • Jardetzky, O.1
  • 44
    • 0024435205 scopus 로고
    • A dynamic model for the structure of acyl carrier protein in solution
    • Kim, Y. & Prestegard, J.H. (1989). A dynamic model for the structure of acyl carrier protein in solution. Biochemistry 28, 8792-8797.
    • (1989) Biochemistry , vol.28 , pp. 8792-8797
    • Kim, Y.1    Prestegard, J.H.2
  • 47
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A. & Davis, D.G. (1985). MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 48
    • 45949117739 scopus 로고
    • Improved techniques for homonuclear rotating-frame and isotropic mixing experiments
    • Rance, M. (1987). Improved techniques for homonuclear rotating-frame and isotropic mixing experiments. J. Magn. Reson. 74, 557-564.
    • (1987) J. Magn. Reson. , vol.74 , pp. 557-564
    • Rance, M.1
  • 49
    • 33845555707 scopus 로고
    • Exchangeable proton NMR without base-line distortion using new strong-pulse sequences
    • Plateau, P. & Gueron, M. (1982). Exchangeable proton NMR without base-line distortion using new strong-pulse sequences. J. Am. Chem. Soc. 104, 7310-7311.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 7310-7311
    • Plateau, P.1    Gueron, M.2
  • 51
    • 0000906068 scopus 로고
    • A new water suppression technique for generating pure-phase spectra with equal excitation over a wide bandwidth
    • Sklenar, V. & Bax, A. (1987). A new water suppression technique for generating pure-phase spectra with equal excitation over a wide bandwidth. J. Magn. Reson. 75, 378-383.
    • (1987) J. Magn. Reson. , vol.75 , pp. 378-383
    • Sklenar, V.1    Bax, A.2
  • 52
    • 0006309162 scopus 로고
    • A simple method for quantitative evaluation of cross-peak intensities in two-dimensional NOE spectra
    • Holak, T.A., Scarsdale, N.J., & Prestegard, J.H. (1987). A simple method for quantitative evaluation of cross-peak intensities in two-dimensional NOE spectra. J. Magn. Reson. 74, 546-549.
    • (1987) J. Magn. Reson. , vol.74 , pp. 546-549
    • Holak, T.A.1    Scarsdale, N.J.2    Prestegard, J.H.3
  • 53
    • 45249128810 scopus 로고
    • Measurement of vicinal couplings from cross peaks in COSY spectra
    • Kim, Y. & Prestegard, J.H. (1989). Measurement of vicinal couplings from cross peaks in COSY spectra. J. Magn. Reson. 84, 9-13.
    • (1989) J. Magn. Reson. , vol.84 , pp. 9-13
    • Kim, Y.1    Prestegard, J.H.2
  • 54
    • 0024559147 scopus 로고
    • Improved strategies for the determination of protein structures from NMR data: The solution structure of acyl carrier protein
    • Holak, T.A., Nilges , M. & Oschkinat, H. (1989). Improved strategies for the determination of protein structures from NMR data: the solution structure of acyl carrier protein. FEBS Lett. 242, 218-224.
    • (1989) FEBS Lett. , vol.242 , pp. 218-224
    • Holak, T.A.1    Nilges, M.2    Oschkinat, H.3
  • 55
    • 0023937834 scopus 로고
    • 7] metallothionein-2a in aqueous solution determined by nuclear magnetic resonance
    • 7] metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J. Mol. Biol. 201, 637-657.
    • (1988) J. Mol. Biol. , vol.201 , pp. 637-657
    • Arseniev, A.1    Wüthrich, K.2
  • 57
    • 0027293559 scopus 로고
    • Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR spectroscopy
    • Brünger, A.T. & Nilges, M. (1993). Computational challenges for macromolecular structure determination by X-ray crystallography and solution NMR spectroscopy. Q. Rev. Biophys. 26, 49-125.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 49-125
    • Brünger, A.T.1    Nilges, M.2
  • 58
    • 0023813070 scopus 로고
    • 3-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations
    • Holak, T.A., Kearsley, S.K., Kim, Y. & Prestegard, J.H. (1988). 3-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations. Biochemistry 27, 6135-6142.
    • (1988) Biochemistry , vol.27 , pp. 6135-6142
    • Holak, T.A.1    Kearsley, S.K.2    Kim, Y.3    Prestegard, J.H.4
  • 60
    • 85030001721 scopus 로고
    • EMBL, Heidelberg
    • Vriend, G. (1991). WHAT IF. EMBL, Heidelberg.
    • (1991) WHAT if
    • Vriend, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.