메뉴 건너뛰기




Volumn 249, Issue 1, 1997, Pages 325-329

A monoclonal antibody induces opening of a coiled coil. Global protection of amide protons from H/D exchange decreases by up to 1000-fold in antibody-bound triple-stranded coiled coil

Author keywords

Coiled coil; Conformational change; Electrospray ionization MS; H D exchange of amide protons; Monoclonal antibody

Indexed keywords

AMINO ACID SEQUENCE; ANTIBODY SPECIFICITY; ANTIGEN ANTIBODY COMPLEX; ARTICLE; CONFORMATIONAL TRANSITION; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN STRUCTURE; THERMODYNAMICS;

EID: 0030810528     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00325.x     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies, D. R. & Cohen, G. H. (1996) Interactions of protein antigens with antibodies, Proc. Natl Acad. Sci. USA 93, 7-12.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 2
    • 0000289157 scopus 로고
    • X-ray crystallography of antibody-peptide complexes
    • Stanfield, R. L. & Wilson, I. A. (1993) X-ray crystallography of antibody-peptide complexes, Immuno Methods 3, 211-221.
    • (1993) Immuno Methods , vol.3 , pp. 211-221
    • Stanfield, R.L.1    Wilson, I.A.2
  • 3
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I. A. & Stanfield, R. L. (1994) Antibody-antigen interactions: new structures and new conformational changes, Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 4
    • 0029561993 scopus 로고
    • Spectroscopic, calorimetric and kinetic demonstration of conformational adaptation in peptide-antibody recognition
    • Leder, L., Berger, C., Bornhauser, S., Wendt, H., Ackermann, F., Jelesarov, I. & Bosshard, H. R. (1995) Spectroscopic, calorimetric and kinetic demonstration of conformational adaptation in peptide-antibody recognition, Biochemistry 34, 16 509-16 518.
    • (1995) Biochemistry , vol.34 , pp. 16509-16518
    • Leder, L.1    Berger, C.2    Bornhauser, S.3    Wendt, H.4    Ackermann, F.5    Jelesarov, I.6    Bosshard, H.R.7
  • 5
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coils
    • Crick, F. H. C. (1953) The packing of alpha-helices: simple coiled-coils, Acta Crystallogr. 6, 689-697.
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 7
    • 0025272940 scopus 로고
    • α-Helical coiled coils and bundles: How to design an α-helical protein
    • Cohen, C. & Parry, D. A. D. (1990) α-Helical coiled coils and bundles: how to design an α-helical protein, Proteins Struct. Funct. Genet. 7, 1-15.
    • (1990) Proteins Struct. Funct. Genet. , vol.7 , pp. 1-15
    • Cohen, C.1    Parry, D.A.D.2
  • 10
    • 0027463314 scopus 로고
    • Protein A antibody-capture ELISA (PACE): An ELISA format to avoid denaturation of surface-adsorbed antigens
    • Ngai, P. K., Ackermann, F., Wendt, H., Savoca, R. & Bosshard, H. R. (1993) Protein A antibody-capture ELISA (PACE): an ELISA format to avoid denaturation of surface-adsorbed antigens, J. Immunol. Methods 158, 267-276.
    • (1993) J. Immunol. Methods , vol.158 , pp. 267-276
    • Ngai, P.K.1    Ackermann, F.2    Wendt, H.3    Savoca, R.4    Bosshard, H.R.5
  • 11
    • 0026317334 scopus 로고
    • Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide
    • Goodman, E. M. & Kim, P. S. (1991) Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide, Biochemistry 30, 11 615-11 620.
    • (1991) Biochemistry , vol.30 , pp. 11615-11620
    • Goodman, E.M.1    Kim, P.S.2
  • 12
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 13
    • 0023481358 scopus 로고
    • Site-directed immobilization of glycoproteins on hydrazide-containing solid supports
    • O'Shannessy, D. & Hoffman, W. L. (1987) Site-directed immobilization of glycoproteins on hydrazide-containing solid supports. Biotechnol. Appl. Biochem. 9, 488-496.
    • (1987) Biotechnol. Appl. Biochem. , vol.9 , pp. 488-496
    • O'Shannessy, D.1    Hoffman, W.L.2
  • 14
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 15
    • 0011946529 scopus 로고
    • α-Helical coild coils: Simple models for self-associating peptide and protein systems
    • Thomas, R. M., Wendt, H., Zampieri, A. & Bosshard, H. R. (1995) α-Helical coild coils: simple models for self-associating peptide and protein systems, Progr. Colloid Polym. Sci. 99, 24-30.
    • (1995) Progr. Colloid Polym. Sci. , vol.99 , pp. 24-30
    • Thomas, R.M.1    Wendt, H.2    Zampieri, A.3    Bosshard, H.R.4
  • 16
    • 0029085077 scopus 로고
    • Characterization of leucine zipper complexes by electrospray ionization mass spectrometry
    • Wendt, H., Dürr, E., Thomas, R. M., Przybylski, M. & Bosshard, H. R. (1995) Characterization of leucine zipper complexes by electrospray ionization mass spectrometry, Protein Sci. 4, 1563-1570.
    • (1995) Protein Sci. , vol.4 , pp. 1563-1570
    • Wendt, H.1    Dürr, E.2    Thomas, R.M.3    Przybylski, M.4    Bosshard, H.R.5
  • 17
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander, S. W. & Mayne, L. (1992) Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR, Annu. Rev. Biophys. Biomol. Struct. 21, 243-265.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 18
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S. W. & Kallenbach, N. R. (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids, Q. Rev. Biophys. 16, 521-655.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 20
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A. & Nielsen, S. O. (1966) Hydrogen exchange in proteins, Adv. Protein Chem. 21, 287-386.
    • (1966) Adv. Protein Chem. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 22
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • Yao, M. & Bolen, D. W. (1995) How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability, Biochemistry 34, 3771-3781.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 23
    • 0025142485 scopus 로고
    • An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR
    • Paterson, Y., Englander, S. W. & Roder, H. (1990) An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR, Science 249, 755-759.
    • (1990) Science , vol.249 , pp. 755-759
    • Paterson, Y.1    Englander, S.W.2    Roder, H.3
  • 24
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L. & Englander, S. W. (1995) Protein folding intermediates: native-state hydrogen exchange, Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 25
    • 0028466243 scopus 로고
    • Protein folding: Solid evidence for molten globules. Novel experimental strategies are providing details of the structures of non-native states of proteins and shedding light on the concept of a 'molten globule' and its relevance to protein folding
    • Dobson, C. M. (1994) Protein folding: Solid evidence for molten globules. Novel experimental strategies are providing details of the structures of non-native states of proteins and shedding light on the concept of a 'molten globule' and its relevance to protein folding, Curr. Biol. 4, 636-640.
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 26
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry
    • Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T. & Dobson, C. M. (1993) Detection of transient protein folding populations by mass spectrometry, Science 262, 896-900.
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 27
    • 0029897362 scopus 로고    scopus 로고
    • Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry
    • Zhang, Z. Q. & Smith, D. L. (1996) Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry, Protein Sci. 5, 1282-1289.
    • (1996) Protein Sci. , vol.5 , pp. 1282-1289
    • Zhang, Z.Q.1    Smith, D.L.2
  • 28
    • 0026455196 scopus 로고
    • Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
    • Mayne, L., Paterson, Y., Cerasoli, D. & Englander, S. W. (1992) Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR, Biochemistry 31, 10 678-10 685.
    • (1992) Biochemistry , vol.31 , pp. 10678-10685
    • Mayne, L.1    Paterson, Y.2    Cerasoli, D.3    Englander, S.W.4
  • 29
    • 0026801082 scopus 로고
    • Long-range changes in a protein antigen due to antigen-antibody interaction
    • Benjamin, D. C., Williams, D. C. Jr, Smith-Gill, S. J. & Rule, G. S. (1992) Long-range changes in a protein antigen due to antigen-antibody interaction, Biochemistry 31, 9539-9545.
    • (1992) Biochemistry , vol.31 , pp. 9539-9545
    • Benjamin, D.C.1    Williams Jr., D.C.2    Smith-Gill, S.J.3    Rule, G.S.4
  • 30
    • 0029968247 scopus 로고    scopus 로고
    • Global hanges in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies
    • Williams, D. C., Benjamin, D. C., Poljak, R. J. & Rule, G. S. (1996) Global hanges in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies, J. Mol. Biol. 257, 866-876.
    • (1996) J. Mol. Biol. , vol.257 , pp. 866-876
    • Williams, D.C.1    Benjamin, D.C.2    Poljak, R.J.3    Rule, G.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.