메뉴 건너뛰기




Volumn 16, Issue 1, 2005, Pages 38-45

LC-mass spectrometry analysis of N- and C-terminal boundary sequences of polypeptide fragments by limited proteolysis

Author keywords

[No Author keywords available]

Indexed keywords

DATA SETS; DOMAIN BOUNDARIES; LIMITED PROTEOLYSIS METHOD; TERTIARY STRUCTURE;

EID: 11844287523     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2004.08.018     Document Type: Article
Times cited : (12)

References (29)
  • 1
    • 0032859140 scopus 로고    scopus 로고
    • Evolution of Protein Function, from a Structural Perspective
    • A.E. Todd, C.A. Orengo, J.M. Thornton Evolution of Protein Function, from a Structural Perspective Curr. Opin. Chem. Biol 3 5 1999 548 556
    • (1999) Curr. Opin. Chem. Biol , vol.3 , Issue.5 , pp. 548-556
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 2
    • 0033970020 scopus 로고    scopus 로고
    • Folding and Binding Cascades: Dynamic Landscapes and Population Shifts
    • S. Kumar, B. Ma, C.J. Tsai, N. Sinha, R. Nussinov Folding and Binding Cascades Dynamic Landscapes and Population Shifts Prot. Sci 9 1 2000 10 19
    • (2000) Prot. Sci , vol.9 , Issue.1 , pp. 10-19
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Sinha, N.4    Nussinov, R.5
  • 3
    • 0021314461 scopus 로고
    • Structural and Functional Aspects of Domain Motions in Proteins
    • W.S. Bennett, R. Huber Structural and Functional Aspects of Domain Motions in Proteins CRC Crit. Rev. Biochem 15 4 1984 291 384
    • (1984) CRC Crit. Rev. Biochem , vol.15 , Issue.4 , pp. 291-384
    • Bennett, W.S.1    Huber, R.2
  • 6
    • 0036358169 scopus 로고    scopus 로고
    • Study of Calcineurin Structure by Limited Proteolysis
    • S.A. Yang, C. Klee Study of Calcineurin Structure by Limited Proteolysis Methods Mol. Biol 172 2002 317 334
    • (2002) Methods Mol. Biol , vol.172 , pp. 317-334
    • Yang, S.A.1    Klee, C.2
  • 8
    • 0023055086 scopus 로고
    • Correlation between Sites of Limited Proteolysis and Segmental Mobility in Thermolysin
    • A. Fontana, G. Fassina, C. Vita, D. Dalzoppo, M. Zamai, M. Zambonin Correlation Between Sites of Limited Proteolysis and Segmental Mobility in Thermolysin Biochemistry 25 8 1986 1847 1851
    • (1986) Biochemistry , vol.25 , Issue.8 , pp. 1847-1851
    • Fontana, A.1    Fassina, G.2    Vita, C.3    Dalzoppo, D.4    Zamai, M.5    Zambonin, M.6
  • 9
    • 0037150075 scopus 로고    scopus 로고
    • Structural Consequences of Tumor-Derived Mutations in P16INK4a Probed by Limited Proteolysis
    • B. Zhang, Z.Y. Peng Structural Consequences of Tumor-Derived Mutations in P16INK4a Probed by Limited Proteolysis Biochemistry 41 20 2002 6293 6302
    • (2002) Biochemistry , vol.41 , Issue.20 , pp. 6293-6302
    • Zhang, B.1    Peng, Z.Y.2
  • 10
    • 0037195926 scopus 로고    scopus 로고
    • The RNA Helicase DbpA Exhibits a Markedly Different Conformation in the ADP-Bound State When Compared with the ATP- or RNA-Bound States
    • A. Henn, S.P. Shi, R. Zarivach, E. Ben-Zeev, I. Sagi The RNA Helicase DbpA Exhibits a Markedly Different Conformation in the ADP-Bound State When Compared with the ATP- or RNA-Bound States J. Biol. Chem 277 48 2002 46559-4665
    • (2002) J. Biol. Chem , vol.277 , Issue.48
    • Henn, A.1    Shi, S.P.2    Zarivach, R.3    Ben-Zeev, E.4    Sagi, I.5
  • 11
    • 0031677656 scopus 로고    scopus 로고
    • Probing the Ligand Binding Domain of the GluR2 Receptor by Proteolysis and Deletion Mutagenesis Defines Domain Boundaries and Yields a Crystalizable Construct
    • G.Q. Chen, Y. Sun, R. Jin, E. Gouaux Probing the Ligand Binding Domain of the GluR2 Receptor by Proteolysis and Deletion Mutagenesis Defines Domain Boundaries and Yields a Crystalizable Construct Prot. Sci 7 12 1998 2623 2630
    • (1998) Prot. Sci , vol.7 , Issue.12 , pp. 2623-2630
    • Chen, G.Q.1    Sun, Y.2    Jin, R.3    Gouaux, E.4
  • 12
    • 0033572798 scopus 로고    scopus 로고
    • Biochemical Properties of a Minimal Functional Domain with ATP-Binding Activity of the NTPase/Helicase of Hepatitis C Virus
    • P. Borowski, R. Kuehl, O. Mueller, L.H. Hwang, J. Schulze zur Wiesch, H. Schmitz Biochemical Properties of a Minimal Functional Domain with ATP-Binding Activity of the NTPase/Helicase of Hepatitis C Virus Eur. J. Biochem 266 3 1999 715 723
    • (1999) Eur. J. Biochem , vol.266 , Issue.3 , pp. 715-723
    • Borowski, P.1    Kuehl, R.2    Mueller, O.3    Hwang, L.H.4    Schulze Zur Wiesch, J.5    Schmitz, H.6
  • 13
    • 0027157228 scopus 로고
    • Production, Purification, and Characterization of the Catalytic Domain of Glucoamylase from Aspergillus niger. Part 1
    • B. Stoffer, T.P. Frandsen, P.K. Busk, P. Schneider, I. Svendsen, B. Svensson Production, Purification, and Characterization of the Catalytic Domain of Glucoamylase from Aspergillus niger. Part 1 Biochem. J 292 1993 197 202
    • (1993) Biochem. J , vol.292 , pp. 197-202
    • Stoffer, B.1    Frandsen, T.P.2    Busk, P.K.3    Schneider, P.4    Svendsen, I.5    Svensson, B.6
  • 14
    • 0036746595 scopus 로고    scopus 로고
    • Protein Secondary Structure and Stability Determined by Combining Exoproteolysis and Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry
    • J. Villanueva, V. Villegas, E. Querol, F.X. Aviles, L. Serrano Protein Secondary Structure and Stability Determined by Combining Exoproteolysis and Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry J. Mass Spectrom 37 9 2002 974 984
    • (2002) J. Mass Spectrom , vol.37 , Issue.9 , pp. 974-984
    • Villanueva, J.1    Villegas, V.2    Querol, E.3    Aviles, F.X.4    Serrano, L.5
  • 15
    • 0034607718 scopus 로고    scopus 로고
    • Coupled Proteolytic and Mass Spectrometry Studies Indicate a Novel Topology for the Glycine Receptor
    • J.F. Leite, A.A. Amoscato, M. Cascio Coupled Proteolytic and Mass Spectrometry Studies Indicate a Novel Topology for the Glycine Receptor J. Biol. Chem 275 18 2000 13683 13689
    • (2000) J. Biol. Chem , vol.275 , Issue.18 , pp. 13683-13689
    • Leite, J.F.1    Amoscato, A.A.2    Cascio, M.3
  • 17
    • 0031985001 scopus 로고    scopus 로고
    • Evidence of Viral Capsid Dynamics Using Limited Proteolysis and Mass Spectrometry
    • B. Bothner, X.F. Dong, L. Bibbs, J.E. Johnson, G. Siuzdak Evidence of Viral Capsid Dynamics Using Limited Proteolysis and Mass Spectrometry J. Biol. Chem 273 2 1998 673 676
    • (1998) J. Biol. Chem , vol.273 , Issue.2 , pp. 673-676
    • Bothner, B.1    Dong, X.F.2    Bibbs, L.3    Johnson, J.E.4    Siuzdak, G.5
  • 18
    • 0037428411 scopus 로고    scopus 로고
    • A Thermally Sensitive Loop in Clostridial Glutamate Dehydrogenase Detected by Limited Proteolysis
    • S. Aghajanian, M. Hovsepyan, K.F. Geoghegan, B.A. Chrunyk, P.C. Engel A Thermally Sensitive Loop in Clostridial Glutamate Dehydrogenase Detected by Limited Proteolysis J. Biol. Chem 278 2 2003 1067 1074
    • (2003) J. Biol. Chem , vol.278 , Issue.2 , pp. 1067-1074
    • Aghajanian, S.1    Hovsepyan, M.2    Geoghegan, K.F.3    Chrunyk, B.A.4    Engel, P.C.5
  • 19
    • 0038162431 scopus 로고    scopus 로고
    • Mass Spectrometry and Non-Covalent Protein-Ligand Complexes: Confirmation of Binding Sites and Changes in Tertiary Structure
    • S.J. Shields, O. Oyeyemi, F.C. Lightstone, R. Balhorn Mass Spectrometry and Non-Covalent Protein-Ligand Complexes Confirmation of Binding Sites and Changes in Tertiary Structure J. Am. Soc. Mass Spectrom 14 5 2003 460 470
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , Issue.5 , pp. 460-470
    • Shields, S.J.1    Oyeyemi, O.2    Lightstone, F.C.3    Balhorn, R.4
  • 20
    • 0344839084 scopus 로고    scopus 로고
    • Analysis of Post-Translational Modification and Characterization of the Domain Structure of Dynamin a from Dictyostelium Discoideum
    • A. Schlosser, B. Klockow, D.J. Manstein, W.D. Lehmann Analysis of Post-Translational Modification and Characterization of the Domain Structure of Dynamin a from Dictyostelium Discoideum J. Mass Spectrom 38 3 2003 277 282
    • (2003) J. Mass Spectrom , vol.38 , Issue.3 , pp. 277-282
    • Schlosser, A.1    Klockow, B.2    Manstein, D.J.3    Lehmann, W.D.4
  • 21
    • 0037461355 scopus 로고    scopus 로고
    • Probing the Dimeric Structure of Porcine Aminoacylase 1 by Mass Spectrometric and Modeling Procedures
    • C. D'Ambrosio, F. Talamo, R.M. Vitale, P. Amodeo, G. Tell, L. Ferrara, A. Scaloni Probing the Dimeric Structure of Porcine Aminoacylase 1 by Mass Spectrometric and Modeling Procedures Biochemistry 42 15 2003 4430 4443
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4430-4443
    • D'Ambrosio, C.1    Talamo, F.2    Vitale, R.M.3    Amodeo, P.4    Tell, G.5    Ferrara, L.6    Scaloni, A.7
  • 22
    • 0028862855 scopus 로고
    • Analysis of the Structural Core of the Human Estrogen Receptor Ligand Binding Domain by Selective Proteolysis/Mass Spectrometric Analysis
    • D.A. Seielstad, K.E. Carlson, P.J. Kushner, G.L. Greene, J.A. Katzenellenbogen Analysis of the Structural Core of the Human Estrogen Receptor Ligand Binding Domain by Selective Proteolysis/Mass Spectrometric Analysis Biochemistry 34 39 1995 12605 12615
    • (1995) Biochemistry , vol.34 , Issue.39 , pp. 12605-12615
    • Seielstad, D.A.1    Carlson, K.E.2    Kushner, P.J.3    Greene, G.L.4    Katzenellenbogen, J.A.5
  • 23
    • 0028817534 scopus 로고
    • Characterization of Post-Translational Modifications of Brain Tubulin by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry: Direct One-Step Analysis of a Limited Subtilisin Digest
    • A. Rudiger, M. Rudiger, K. Weber, D. Schomburg Characterization of Post-Translational Modifications of Brain Tubulin by Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Direct One-Step Analysis of a Limited Subtilisin Digest Anal. Biochem 224 2 1995 532 537
    • (1995) Anal. Biochem , vol.224 , Issue.2 , pp. 532-537
    • Rudiger, A.1    Rudiger, M.2    Weber, K.3    Schomburg, D.4
  • 24
    • 0036965184 scopus 로고    scopus 로고
    • Domain Organization of D-AKAP-2 Revealed by Enhanced Deuterium Exchange-Mass Spectrometry (DXMS)
    • Y. Hamuro, L. Burns, J. Canaves, R. Hoffman, S. Taylor, V. Woods Domain Organization of D-AKAP-2 Revealed by Enhanced Deuterium Exchange-Mass Spectrometry (DXMS) J. Mol. Biol 321 4 2002 703 714
    • (2002) J. Mol. Biol , vol.321 , Issue.4 , pp. 703-714
    • Hamuro, Y.1    Burns, L.2    Canaves, J.3    Hoffman, R.4    Taylor, S.5    Woods, V.6
  • 25
    • 0032544207 scopus 로고    scopus 로고
    • Identification of the Binding Surface on β-Lactamase for Groel by Limited Proteolysis and MALDI-Mass Spectrometry
    • P. Gervasoni, W. Staudenmann, P. James, A. Pluckthun Identification of the Binding Surface on β-Lactamase for Groel by Limited Proteolysis and MALDI-Mass Spectrometry Biochemistry 37 33 1998 11660 11669
    • (1998) Biochemistry , vol.37 , Issue.33 , pp. 11660-11669
    • Gervasoni, P.1    Staudenmann, W.2    James, P.3    Pluckthun, A.4
  • 26
    • 0042324395 scopus 로고    scopus 로고
    • Analysis of the Effect of Potato Carboxypeptidase Inhibitor Pro-Sequence on the Folding of the Mature Protein
    • S. Bronsoms, J. Villanueva, F. Canals, E. Querol, F.X. Aviles Analysis of the Effect of Potato Carboxypeptidase Inhibitor Pro-Sequence on the Folding of the Mature Protein Eur. J. Biochem 270 17 2003 3641 3650
    • (2003) Eur. J. Biochem , vol.270 , Issue.17 , pp. 3641-3650
    • Bronsoms, S.1    Villanueva, J.2    Canals, F.3    Querol, E.4    Aviles, F.X.5
  • 27
    • 0029004044 scopus 로고
    • Probing the Solution Structure of the DNA-Binding Protein Max by a Combination of Proteolysis and Mass Spectrometry
    • S.L. Cohen, A.R. Ferre-D'Amare, S.K. Burley, B.T. Chait Probing the Solution Structure of the DNA-Binding Protein Max by a Combination of Proteolysis and Mass Spectrometry Prot. Sci 4 6 1995 1088 1099
    • (1995) Prot. Sci , vol.4 , Issue.6 , pp. 1088-1099
    • Cohen, S.L.1    Ferre-D'Amare, A.R.2    Burley, S.K.3    Chait, B.T.4
  • 28
    • 0036084052 scopus 로고    scopus 로고
    • Description of the Topographical Changes Associated to the Different Stages of the DSBA Catalytic Cycle
    • F. Vinci, J. Couprie, P. Pucci, E. Quemeneur, M. Moutiez Description of the Topographical Changes Associated to the Different Stages of the DSBA Catalytic Cycle Prot. Sci 11 7 2002 1600 1612
    • (2002) Prot. Sci , vol.11 , Issue.7 , pp. 1600-1612
    • Vinci, F.1    Couprie, J.2    Pucci, P.3    Quemeneur, E.4    Moutiez, M.5
  • 29
    • 0030761239 scopus 로고    scopus 로고
    • Transforming Growth Factor (TGF-β)-Specific Signaling by Chimeric TGF-β Type II Receptor with Intracellular Domain of Activin Type IIb Receptor
    • U. Persson, S. Souchelnytskyi, P. Franzen, K. Miyazono, P. ten Dijke, C.H. Heldin Transforming Growth Factor (TGF-β)-Specific Signaling by Chimeric TGF-β Type II Receptor with Intracellular Domain of Activin Type IIb Receptor J. Biol. Chem 272 34 1997 21187 21194
    • (1997) J. Biol. Chem , vol.272 , Issue.34 , pp. 21187-21194
    • Persson, U.1    Souchelnytskyi, S.2    Franzen, P.3    Miyazono, K.4    Ten Dijke, P.5    Heldin, C.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.