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Volumn 5, Issue 7, 1996, Pages 1301-1315

A recipe for designing water-soluble, β-sheet-forming peptides

Author keywords

CD; folding; NMR; peptide; self association; sheet structure

Indexed keywords

GROWTH PROMOTOR; GROWTH RELATED PROTEIN; INTERLEUKIN 8; PEPTIDE; THROMBOCYTE FACTOR 4; UNCLASSIFIED DRUG;

EID: 0029927321     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050709     Document Type: Article
Times cited : (90)

References (81)
  • 1
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri AS, Kinton DP, Byrd RA. 1995. Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J Am Chem Soc 117:7566-7567.
    • (1995) J Am Chem Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Kinton, D.P.2    Byrd, R.A.3
  • 2
    • 0023550277 scopus 로고
    • Constitutive overexpression of a growth-regulated gene in transformed Chinese hamster and human cells
    • Anisowicz A, Bardwell L, Sager R. 1987. Constitutive overexpression of a growth-regulated gene in transformed Chinese hamster and human cells. Proc Natl Acad Sci USA 84:1188-7192.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1188-7192
    • Anisowicz, A.1    Bardwell, L.2    Sager, R.3
  • 4
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax A, Davis DG. 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
  • 5
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A
    • Bierzynski A, Kim PS, Baldwin RL. 1982. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc Natl Acad Sci USA 79:2470-2414.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 2470-12414
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 6
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable β-hairpin in aqueous solution
    • Blanco FJ, Rivas G, Serrano L. 1994. A short linear peptide that folds into a native stable β-hairpin in aqueous solution. Struct Biol 7:584-590.
    • (1994) Struct Biol , vol.7 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 10
    • 0025779255 scopus 로고
    • Human platelet factor-4 subunit association/dissociation thermodynamics and kinetics
    • Chen MJ, Mayo KH. 1991. Human platelet factor-4 subunit association/dissociation thermodynamics and kinetics. Biochemistry 50:6402-6411.
    • (1991) Biochemistry , vol.50 , pp. 6402-6411
    • Chen, M.J.1    Mayo, K.H.2
  • 13
    • 0024515763 scopus 로고
    • Protein design, a minimalist approach
    • DeGrado W, Wasserman Z, Lear J. 1989. Protein design, a minimalist approach. Science 243:622-628.
    • (1989) Science , vol.243 , pp. 622-628
    • DeGrado, W.1    Wasserman, Z.2    Lear, J.3
  • 15
    • 0029400890 scopus 로고
    • Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2
    • Dingley AJ, Mackay JP, Chapman BE, Morris MB, Kuchel PW, Hambly, BD, King GF. 1995. Measuring protein self-association using pulsed-field-gradient NMR spectroscopy: Application to myosin light chain 2. J Biomol NMR 6:321-328.
    • (1995) J Biomol NMR , vol.6 , pp. 321-328
    • Dingley, A.J.1    Mackay, J.P.2    Chapman, B.E.3    Morris, M.B.4    Kuchel, P.W.5    Hambly, B.D.6    King, G.F.7
  • 16
    • 0001684047 scopus 로고
    • Measurement of the rotational diffusion coefficients of lysozyme in solution
    • Dubin SB, Clark NA, Benedek GB. 1971. Measurement of the rotational diffusion coefficients of lysozyme in solution. J Chem Phys 54:5158-5165.
    • (1971) J Chem Phys , vol.54 , pp. 5158-5165
    • Dubin, S.B.1    Clark, N.A.2    Benedek, G.B.3
  • 19
    • 0028224544 scopus 로고
    • De novo design and structural characterization of an α-helical hairpin peptide: A model system for the study of protein folding intermediates
    • Fezoui J, Weaver DL, Osterhout JJ. 1994. De novo design and structural characterization of an α-helical hairpin peptide: A model system for the study of protein folding intermediates. Proc Natl Acad Sci USA 91:3675-3679.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3675-3679
    • Fezoui, J.1    Weaver, D.L.2    Osterhout, J.J.3
  • 20
    • 44949277996 scopus 로고
    • A PFG NMR experiment for accurate diffusion and flow studies in the presence of eddy currents
    • Gibbs SJ, Johnson CS. 1991. A PFG NMR experiment for accurate diffusion and flow studies in the presence of eddy currents. J Magn Reson 93:395-402.
    • (1991) J Magn Reson , vol.93 , pp. 395-402
    • Gibbs, S.J.1    Johnson, C.S.2
  • 21
    • 0029044454 scopus 로고
    • B/PI-derived peptides: Synergistic effects in tethered bactericidal and endotoxin neutralizing peptides
    • Gray BH, Haseman J, Mayo KH. 1995. B/PI-derived peptides: Synergistic effects in tethered bactericidal and endotoxin neutralizing peptides. Biochim Biophys Acta 1244:185-190.
    • (1995) Biochim Biophys Acta , vol.1244 , pp. 185-190
    • Gray, B.H.1    Haseman, J.2    Mayo, K.H.3
  • 22
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield N, Fasman GD. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 5:4108-4116.
    • (1969) Biochemistry , vol.5 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 23
    • 0025335121 scopus 로고
    • Design and synthesis of a peptide having chymotrypsin-like esterase activity
    • Hahn K, Klis W, Stewart J. 1990. Design and synthesis of a peptide having chymotrypsin-like esterase activity. Science 248:1544-1547.
    • (1990) Science , vol.248 , pp. 1544-1547
    • Hahn, K.1    Klis, W.2    Stewart, J.3
  • 24
    • 0027177971 scopus 로고
    • Metal ion-dependent modulation of the dynamics of a designed protein
    • Handel TM, Williams SA, DeGrado WF. 1993. Metal ion-dependent modulation of the dynamics of a designed protein. Science 257:879-885.
    • (1993) Science , vol.257 , pp. 879-885
    • Handel, T.M.1    Williams, S.A.2    DeGrado, W.F.3
  • 25
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury PB, Kim PS, Alber T. 1994. Crystal structure of an isoleucine-zipper trimer. Nature 377:80-83.
    • (1994) Nature , vol.377 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 26
    • 0025040232 scopus 로고
    • Denovo design, expression, and characterization of Felix: A four-helix bundle protein of native-like sequence
    • Hecht M, Richardson J, Richardson D, Ogden R. 1990. Denovo design, expression, and characterization of Felix: A four-helix bundle protein of native-like sequence. Science 249:884-891.
    • (1990) Science , vol.249 , pp. 884-891
    • Hecht, M.1    Richardson, J.2    Richardson, D.3    Ogden, R.4
  • 27
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch ZS, Tidor B. 1994. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci 3:211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 28
    • 0022473126 scopus 로고
    • Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin
    • Holt JC, Harris ME, Holt A, Lange E, Henschen A, Niewiarowski S. 1986. Characterization of human platelet basic protein, a precursor form of low-affinity platelet factor 4 and beta-thromboglobulin. Biochemistry 25:1988-1996.
    • (1986) Biochemistry , vol.25 , pp. 1988-1996
    • Holt, J.C.1    Harris, M.E.2    Holt, A.3    Lange, E.4    Henschen, A.5    Niewiarowski, S.6
  • 29
    • 0022049305 scopus 로고
    • Biochemistry of alpha granule proteins
    • Holt JC, Niewiarowski S. 1985. Biochemistry of alpha granule proteins. Sem Hematol 22:151-163.
    • (1985) Sem Hematol , vol.22 , pp. 151-163
    • Holt, J.C.1    Niewiarowski, S.2
  • 30
    • 0027984190 scopus 로고
    • Synthetic peptides probe folding initiation sites in platelet factor-4: Stable chain reversal found within the hydrophobic sequence LIATLKNGRKISL
    • Ilyina E, Milius R, Mayo KH. 1994. Synthetic peptides probe folding initiation sites in platelet factor-4: Stable chain reversal found within the hydrophobic sequence LIATLKNGRKISL. Biochemistry 33:13436-13444.
    • (1994) Biochemistry , vol.33 , pp. 13436-13444
    • Ilyina, E.1    Milius, R.2    Mayo, K.H.3
  • 31
    • 0028959874 scopus 로고
    • Multiple native-like conformations trapped via self-association-induced hydrophobic collapse of the 33-residue beta-sheet domain from platelet factor 4
    • Ilyina E, Mayo KH. 1995. Multiple native-like conformations trapped via self-association-induced hydrophobic collapse of the 33-residue beta-sheet domain from platelet factor 4. Biochem J 306:407-419.
    • (1995) Biochem J , vol.306 , pp. 407-419
    • Ilyina, E.1    Mayo, K.H.2
  • 32
    • 0025876740 scopus 로고
    • Protein folding: Local structures, domains, subunits, and assemblies
    • Jaenicke R. 1991. Protein folding: Local structures, domains, subunits, and assemblies. Biochemistry 30:3147-3161.
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 34
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J, Meier B, Backman P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71:4546-4550.
    • (1979) J Chem Phys , vol.71 , pp. 4546-4550
    • Jeener, J.1    Meier, B.2    Backman, P.3    Ernst, R.R.4
  • 35
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson WC Jr. 1990. Protein secondary structure and circular dichroism: A practical guide. Proteins Struct Funct Genet 7:205-214.
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 36
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamteker S, Schiffer JM, Xiong H, Babik JM, Hecht MH. 1993. Protein design by binary patterning of polar and nonpolar amino acids. Science 262:1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamteker, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 37
    • 0027411181 scopus 로고
    • Thermodynamic β-sheet propensities measured using a zinc-finger host peptide
    • Kim CA, Berg JM. 1993. Thermodynamic β-sheet propensities measured using a zinc-finger host peptide. Nature 362:267-270.
    • (1993) Nature , vol.362 , pp. 267-270
    • Kim, C.A.1    Berg, J.M.2
  • 38
    • 0028268619 scopus 로고
    • Solution structure of a de novo helical protein by 2D-NMR spectroscopy
    • Kuroda Y, Nakai T, Ohkubo T. 1994. Solution structure of a de novo helical protein by 2D-NMR spectroscopy. J Mol Biol 236:862-868.
    • (1994) J Mol Biol , vol.236 , pp. 862-868
    • Kuroda, Y.1    Nakai, T.2    Ohkubo, T.3
  • 39
    • 0029020822 scopus 로고
    • NMR analysis of the selective complexation of the cis and trans isomers of phenylanylproline by β-cyclodextrin
    • Lin M, Jayawickrama A, Rose RA, DelViscio JA, Larive CK. 1995. NMR analysis of the selective complexation of the cis and trans isomers of phenylanylproline by β-cyclodextrin. Anal Chim Acta 307:449-457.
    • (1995) Anal Chim Acta , vol.307 , pp. 449-457
    • Lin, M.1    Jayawickrama, A.2    Rose, R.A.3    DelViscio, J.A.4    Larive, C.K.5
  • 40
    • 0028306360 scopus 로고
    • Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4
    • Lumb KJ, Carr CM, Kim PS. 1994. Subdomain folding of the coiled coil leucine zipper from the bZIP transcriptional activator GCN4. Biochemistry 33:7361-7367.
    • (1994) Biochemistry , vol.33 , pp. 7361-7367
    • Lumb, K.J.1    Carr, C.M.2    Kim, P.S.3
  • 41
    • 0029030233 scopus 로고
    • Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper
    • Lumb KJ, Kim PS. 1995. Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper. Science 265:436-438.
    • (1995) Science , vol.265 , pp. 436-438
    • Lumb, K.J.1    Kim, P.S.2
  • 42
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A. 1985. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J Magn Reson 89:393-399.
    • (1985) J Magn Reson , vol.89 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 44
    • 0029153681 scopus 로고
    • NMR solution structure of the 32-kDa platelet factor 4 ELR-mo:if N-terminal chimera: A symmetric tetramer
    • Mayo KH, Roongta V, Ilyina E, Milius R, Barker S, Quinlan C, La Rosa G, Daly TJ. 1995. NMR solution structure of the 32-kDa platelet factor 4 ELR-mo:if N-terminal chimera: A symmetric tetramer. Biochemistry 34:11399-11409.
    • (1995) Biochemistry , vol.34 , pp. 11399-11409
    • Mayo, K.H.1    Roongta, V.2    Ilyina, E.3    Milius, R.4    Barker, S.5    Quinlan, C.6    La Rosa, G.7    Daly, T.J.8
  • 46
    • 0026776079 scopus 로고
    • Biology and biochemistry of the chemokines: A family of chemotactic and inflammatory cytokines
    • Miller MD, Krangel MS. 1992. Biology and biochemistry of the chemokines: A family of chemotactic and inflammatory cytokines. Crit Rev Immunol 72:17-46.
    • (1992) Crit Rev Immunol , vol.72 , pp. 17-46
    • Miller, M.D.1    Krangel, M.S.2
  • 47
    • 0042936805 scopus 로고
    • Self-diffusion in normal and heavy water in the range of 1-45°
    • Mills R. 1973. Self-diffusion in normal and heavy water in the range of 1-45° J Phys Chem 77:685-688.
    • (1973) J Phys Chem , vol.77 , pp. 685-688
    • Mills, R.1
  • 48
    • 0028176595 scopus 로고
    • Measurement of the beta-sheet-forming propensities of amino acids
    • Minor DL Jr, Kim PS. 1994a. Measurement of the beta-sheet-forming propensities of amino acids. Nature 367:660-663.
    • (1994) Nature , vol.367 , pp. 660-663
    • Minor Jr., D.L.1    Kim, P.S.2
  • 49
    • 0027998757 scopus 로고
    • Context is a major determinant of beta-sheet propensity
    • Minor DL Jr, Kim PS. 1994b. Context is a major determinant of beta-sheet propensity. Nature 371:264-267.
    • (1994) Nature , vol.371 , pp. 264-267
    • Minor Jr., D.L.1    Kim, P.S.2
  • 50
    • 0028988836 scopus 로고
    • Side-chain determinants of beta-sheet stability
    • Otzen DE, Fersht AR. 1995. Side-chain determinants of beta-sheet stability. Biochemistry 34:5718-5724.
    • (1995) Biochemistry , vol.34 , pp. 5718-5724
    • Otzen, D.E.1    Fersht, A.R.2
  • 51
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini U, Sørensen OW, Ernst RR. 1982. Multiple quantum filters for elucidating NMR coupling networks. J Am Chem Soc 704:6800-6801.
    • (1982) J Am Chem Soc , vol.704 , pp. 6800-6801
    • Piantini, U.1    Sørensen, O.W.2    Ernst, R.R.3
  • 52
    • 0002876857 scopus 로고
    • The molten globule state
    • Nall BT, Dill KA, eds. Washington, DC: American Association for the Advancement of Science
    • Ptitsyn OB, Misotnov GV. 1991. The molten globule state. In: Nall BT, Dill KA, eds. Conformations and forces in protein folding. Washington, DC: American Association for the Advancement of Science. pp 155-168.
    • (1991) Conformations and Forces in Protein Folding , pp. 155-168
    • Ptitsyn, O.B.1    Misotnov, G.V.2
  • 54
    • 0023812695 scopus 로고
    • Characterization of a helical protein designed from first principles
    • Regan L, DeGrado W. 1988. Characterization of a helical protein designed from first principles. Science 241:976-978.
    • (1988) Science , vol.241 , pp. 976-978
    • Regan, L.1    DeGrado, W.2
  • 57
    • 0023254096 scopus 로고
    • Induction of mRNA for a serine protease and a beta-thromboglobulin-like protein in mitogen-stimulated human leukocytes
    • Schmid J, Weissmann C. 1987. Induction of mRNA for a serine protease and a beta-thromboglobulin-like protein in mitogen-stimulated human leukocytes. J Immunol 139:250-256.
    • (1987) J Immunol , vol.139 , pp. 250-256
    • Schmid, J.1    Weissmann, C.2
  • 58
    • 0028865129 scopus 로고
    • A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-soluble non-native β-hairpin
    • Searle MS, Williams DH, Packman LC. 1995. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-soluble non-native β-hairpin. Nature Struct Biol 2:999-1006.
    • (1995) Nature Struct Biol , vol.2 , pp. 999-1006
    • Searle, M.S.1    Williams, D.H.2    Packman, L.C.3
  • 59
    • 0003062277 scopus 로고
    • Simplification of NMR spectra by filtration through multiple-quantum coherence
    • Shaka AJ, Freeman R. 1983. Simplification of NMR spectra by filtration through multiple-quantum coherence. J Magn Reson 51:169-173.
    • (1983) J Magn Reson , vol.51 , pp. 169-173
    • Shaka, A.J.1    Freeman, R.2
  • 61
    • 0028792105 scopus 로고
    • Guidelines for protein design: The energetics of β sheet side chain interactions
    • Smith CK, Regan L. 1995. Guidelines for protein design: The energetics of β sheet side chain interactions. Science 270:980-982.
    • (1995) Science , vol.270 , pp. 980-982
    • Smith, C.K.1    Regan, L.2
  • 62
    • 0028175780 scopus 로고
    • A thermodynamic scale for the β-sheet forming tendencies of the amino acids
    • Smith CK, Withka JM, Regan L. 1994. A thermodynamic scale for the β-sheet forming tendencies of the amino acids. Biochemistry 33:5510-5517.
    • (1994) Biochemistry , vol.33 , pp. 5510-5517
    • Smith, C.K.1    Withka, J.M.2    Regan, L.3
  • 63
  • 64
    • 2642628181 scopus 로고
    • A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants
    • States DJ, Haberkorn RA, Ruben DJ. 1982. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J Magn Reson 45:286-293.
    • (1982) J Magn Reson , vol.45 , pp. 286-293
    • States, D.J.1    Haberkorn, R.A.2    Ruben, D.J.3
  • 65
    • 0024555819 scopus 로고
    • The three-dimensional structure of bovine platelet factor 4 at 3.0-Å resolution
    • St. Charles R, Walz DA, Edwards BFP. 1989. The three-dimensional structure of bovine platelet factor 4 at 3.0-Å resolution. J Biol Chem 264: 2092-2099.
    • (1989) J Biol Chem , vol.264 , pp. 2092-2099
    • St. Charles, R.1    Walz, D.A.2    Edwards, B.F.P.3
  • 67
    • 33646376290 scopus 로고
    • Spin diffusion measurements: Spin echoes in the presence of a time dependent field gradient
    • Steyskal EO, Tanner JE. 1965. Spin diffusion measurements: Spin echoes in the presence of a time dependent field gradient. J Chem Phys 42: 288-292.
    • (1965) J Chem Phys , vol.42 , pp. 288-292
    • Steyskal, E.O.1    Tanner, J.E.2
  • 68
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • Struthers MD, Cheng RP, Imperiali B. 1996. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science 271:342-345.
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 70
    • 0028598623 scopus 로고
    • Determinants of protein side-chain packing
    • Tanimura R, Kidera A, Nakamura H. 1994. Determinants of protein side-chain packing. Protein Sci 3:2358-2365.
    • (1994) Protein Sci , vol.3 , pp. 2358-2365
    • Tanimura, R.1    Kidera, A.2    Nakamura, H.3
  • 71
    • 0018339645 scopus 로고
    • The translational friction coefficient of proteins
    • Teller DC, Swanson E, de Haen C. 1979. The translational friction coefficient of proteins. Methods Enzymol 61:103-124.
    • (1979) Methods Enzymol , vol.61 , pp. 103-124
    • Teller, D.C.1    Swanson, E.2    De Haen, C.3
  • 73
    • 0024831225 scopus 로고
    • Effects of the neutrophil-activating peptide NAP-2, platelet basic protein, connective tissue-activating peptide III and platelet factor-4 on human neutrophils
    • Walz A, Dewald B, von Tscharner V, Baggiolini M. 1989. Effects of the neutrophil-activating peptide NAP-2, platelet basic protein, connective tissue-activating peptide III and platelet factor-4 on human neutrophils. J Exp Med 170:1745-1750.
    • (1989) J Exp Med , vol.170 , pp. 1745-1750
    • Walz, A.1    Dewald, B.2    Von Tscharner, V.3    Baggiolini, M.4
  • 74
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous DV, Johnson WC. 1994. Importance of environment in determining secondary structure in proteins. Biochemistry 33:2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson, W.C.2
  • 76
    • 0000498521 scopus 로고
    • Concentration dependence of the diffusion coefficient of a dimerizing protein: Bovine pancreatic trypsin inhibitor
    • Wills PR, Georgalis Y. 1981. Concentration dependence of the diffusion coefficient of a dimerizing protein: Bovine pancreatic trypsin inhibitor. J Phys Chem 85:3978-3984.
    • (1981) J Phys Chem , vol.85 , pp. 3978-3984
    • Wills, P.R.1    Georgalis, Y.2
  • 77
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart DS, Sykes BD, Richards FM. 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
  • 78
    • 0024848284 scopus 로고
    • Macrophage inflammatory proteins 1 and 2: Members of a novel superfamily of cytokines
    • Wolpe SD, Cerami A. 1989. Macrophage inflammatory proteins 1 and 2: Members of a novel superfamily of cytokines. FASEB J 3:2565-2573.
    • (1989) FASEB J , vol.3 , pp. 2565-2573
    • Wolpe, S.D.1    Cerami, A.2
  • 80
    • 0028309466 scopus 로고
    • Engineering of betabellin 14D: Disulfide-induced folding of a β-sheet protein
    • Yan Y, Erickson BW. 1994. Engineering of betabellin 14D: Disulfide-induced folding of a β-sheet protein. Protein Sci 3:1069-1073.
    • (1994) Protein Sci , vol.3 , pp. 1069-1073
    • Yan, Y.1    Erickson, B.W.2
  • 81
    • 0028064302 scopus 로고
    • Crystal structure of recombinant human platelet factor 4
    • Zhang X, Chen L, Bancroft DP. 1994. Crystal structure of recombinant human platelet factor 4. Biochemistry 33:8361-8366.
    • (1994) Biochemistry , vol.33 , pp. 8361-8366
    • Zhang, X.1    Chen, L.2    Bancroft, D.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.