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Volumn 10, Issue 6, 2014, Pages 2404-2414

Determination of orientation and adsorption-induced changes in the tertiary structure of proteins on material surfaces by chemical modification and peptide mapping

Author keywords

Chemical labeling; Mass spectrometry; Protein structural change; Protein protein interaction; Protein surface interaction

Indexed keywords

ADSORPTION; CHEMICAL MODIFICATION; ESTERS; FUSED SILICA; GLASS; MAPPING; MASS SPECTROMETRY; PEPTIDES; SURFACE PROPERTIES;

EID: 84899650577     PISSN: 17427061     EISSN: 18787568     Source Type: Journal    
DOI: 10.1016/j.actbio.2014.01.027     Document Type: Article
Times cited : (22)

References (30)
  • 1
    • 36249028919 scopus 로고    scopus 로고
    • In: Biomaterials: Protein-surface interactions
    • In: Bowlin GL, Wnek GE, editors New York, NY: Informa Healthcare
    • Latour RA. In: Biomaterials: protein-surface interactions. In: Bowlin GL, Wnek GE, editors. The encyclopedia of biomaterials and bioengineering. New York, NY: Informa Healthcare; 2008. p. 270-84.
    • (2008) The Encyclopedia of Biomaterials and Bioengineering , pp. 270-284
    • Latour, R.A.1
  • 2
    • 79951770246 scopus 로고    scopus 로고
    • Understanding protein adsorption phenomena at solid surfaces
    • Rabe M, Verdes D, Seeger S. Understanding protein adsorption phenomena at solid surfaces. Adv Colloid Interface Sci 2011;162:87-106.
    • (2011) Adv Colloid Interface Sci , vol.162 , pp. 87-106
    • Rabe, M.1    Verdes, D.2    Seeger, S.3
  • 3
    • 1342302795 scopus 로고    scopus 로고
    • The interaction of proteins with solid surfaces
    • Gray JJ. The interaction of proteins with solid surfaces. Curr Opin Struct Biol 2004;14:110-5.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 110-115
    • Gray, J.J.1
  • 4
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton JT, McLean LR. Spectroscopic methods for analysis of protein secondary structure. Anal Biochem 2000;277:167-76.
    • (2000) Anal Biochem , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 5
    • 33744783395 scopus 로고    scopus 로고
    • Determination of the orientation of adsorbed cytochrome c on carboxyalkanethiol self-assembled monolayers by in situ differential modification
    • Xu JS, Bowden EF. Determination of the orientation of adsorbed cytochrome c on carboxyalkanethiol self-assembled monolayers by in situ differential modification. J Am Chem Soc 2006;128:6813-22.
    • (2006) J Am Chem Soc , vol.128 , pp. 6813-6822
    • Xu, J.S.1    Bowden, E.F.2
  • 6
    • 34447265050 scopus 로고    scopus 로고
    • Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces
    • Scott EA, Elbert DL. Mass spectrometric mapping of fibrinogen conformations at poly(ethylene terephthalate) interfaces. Biomaterials 2007;28:3904-17.
    • (2007) Biomaterials , vol.28 , pp. 3904-3917
    • Scott, E.A.1    Elbert, D.L.2
  • 7
    • 68649099249 scopus 로고    scopus 로고
    • Probing the conformation and orientation of adsorbed enzymes using side-chain modification
    • Fears KP, Sivaraman B, Powell GL, Wu Y, Latour RA. Probing the conformation and orientation of adsorbed enzymes using side-chain modification. Langmuir 2009;25:9319-27.
    • (2009) Langmuir , vol.25 , pp. 9319-9327
    • Fears, K.P.1    Sivaraman, B.2    Powell, G.L.3    Wu, Y.4    Latour, R.A.5
  • 8
    • 69849100869 scopus 로고    scopus 로고
    • Probing protein structure by amino acid-specific covalent labeling and mass spectrometry
    • Mendoza VL, Vachet RW. Probing protein structure by amino acid-specific covalent labeling and mass spectrometry. Mass Spectrom Rev 2009;28: 785-815.
    • (2009) Mass Spectrom Rev , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 9
    • 1842868694 scopus 로고    scopus 로고
    • Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes
    • Yan X, Watson J, Ho PS, Deinzer ML. Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes. Mol Cell Proteomics 2004;3:10-23.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 10-23
    • Yan, X.1    Watson, J.2    Ho, P.S.3    Deinzer, M.L.4
  • 10
    • 16344383328 scopus 로고    scopus 로고
    • Application of residue distribution along the sequence for discriminating outer membrane proteins
    • Gromiha MM, Ahmad S, Suwa M. Application of residue distribution along the sequence for discriminating outer membrane proteins. Comput Biol Chem 2005;29:135-42.
    • (2005) Comput Biol Chem , vol.29 , pp. 135-142
    • Gromiha, M.M.1    Ahmad, S.2    Suwa, M.3
  • 12
    • 79955574707 scopus 로고    scopus 로고
    • A new strategy for ionization enhancement by derivatization for mass spectrometry
    • Iwasaki Y, Nakano Y, Mochizuki K, Nomoto M, Takahashi Y, Ito R, et al. A new strategy for ionization enhancement by derivatization for mass spectrometry. J Chromatogr B 2011;879:1159-65.
    • (2011) J Chromatogr B , vol.879 , pp. 1159-1165
    • Iwasaki, Y.1    Nakano, Y.2    Mochizuki, K.3    Nomoto, M.4    Takahashi, Y.5    Ito, R.6
  • 14
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • Scopes RK. Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 1974;59:277-82.
    • (1974) Anal Biochem , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 15
    • 84881267612 scopus 로고    scopus 로고
    • Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm
    • Anthis NJ, Clore GM. Sequence-specific determination of protein and peptide concentrations by absorbance at 205 nm. Protein Sci 2013;22:851-8.
    • (2013) Protein Sci , vol.22 , pp. 851-858
    • Anthis, N.J.1    Clore, G.M.2
  • 16
    • 33646934762 scopus 로고    scopus 로고
    • Spectrophotometric determination of protein concentration
    • New York: Wiley
    • Simonian MH. Spectrophotometric determination of protein concentration. Current protocols in cell biology. New York: Wiley; 2001.
    • (2001) Current Protocols in Cell Biology
    • Simonian, M.H.1
  • 17
    • 71549152820 scopus 로고    scopus 로고
    • Quantitation of protein
    • In: Richard RB, Murray PD, editors New York: Academic Press
    • Noble JE, Bailey MJA. Quantitation of protein. In: Richard RB, Murray PD, editors. Methods in enzymology. New York: Academic Press; 2009. p. 73-95.
    • (2009) Methods in Enzymology , pp. 73-95
    • Noble, J.E.1    Bailey, M.J.A.2
  • 18
    • 84878975183 scopus 로고    scopus 로고
    • Quantification of the influence of protein- protein interactions on adsorbed protein structure and bioactivity
    • Wei Y, Thyparambil AA, Latour RA. Quantification of the influence of protein- protein interactions on adsorbed protein structure and bioactivity. Colloids Surf B 2013;110:363-71.
    • (2013) Colloids Surf B , vol.110 , pp. 363-371
    • Wei, Y.1    Thyparambil, A.A.2    Latour, R.A.3
  • 19
  • 20
    • 33947733294 scopus 로고    scopus 로고
    • Use of the arginine-specific butane dione/phenylboronic acid tag for analysis of peptides and protein digests using matrix-assisted laser desorption/ionization mass spectrometry
    • Leitner A, Amon S, Rizzi A, Lindner W. Use of the arginine-specific butane dione/phenylboronic acid tag for analysis of peptides and protein digests using matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 2007;21:1321-30.
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 1321-1330
    • Leitner, A.1    Amon, S.2    Rizzi, A.3    Lindner, W.4
  • 21
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass-spectrometric peptide-mapping
    • Suckau D, Mak M, Przybylski M. Protein surface topology-probing by selective chemical modification and mass-spectrometric peptide-mapping. Proc Natl Acad Sci USA 1992;89:5630-4.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 22
    • 79851513173 scopus 로고    scopus 로고
    • The beginning of a beautiful friendship: Cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes
    • Rappsilber J. The beginning of a beautiful friendship: cross-linking/mass spectrometry and modelling of proteins and multi-protein complexes. J Struct Biol 2011;173:530-40.
    • (2011) J Struct Biol , vol.173 , pp. 530-540
    • Rappsilber, J.1
  • 23
    • 0038309560 scopus 로고    scopus 로고
    • Analysis of accessible surface of residues in proteins
    • Lins L, Thomas A, Brasseur R. Analysis of accessible surface of residues in proteins. Protein Sci 2003;12:1406-17.
    • (2003) Protein Sci , vol.12 , pp. 1406-1417
    • Lins, L.1    Thomas, A.2    Brasseur, R.3
  • 25
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • Refaee M, Tezuka T, Akasaka K, Williamson MP. Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J Mol Biol 2003;327:857-65.
    • (2003) J Mol Biol , vol.327 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 27
    • 0018093765 scopus 로고
    • Conformational preferences of amino-acids in globular proteins
    • Levitt M. Conformational preferences of amino-acids in globular proteins. Biochemistry (US) 1978;17:4277-84.
    • (1978) Biochemistry (US) , vol.17 , pp. 4277-4284
    • Levitt, M.1
  • 28
    • 0034595515 scopus 로고    scopus 로고
    • Protein packing: Dependence on protein size, secondary structure and amino acid composition
    • Fleming PJ, Richards FM. Protein packing: dependence on protein size, secondary structure and amino acid composition. J Mol Biol 2000;299: 487-98.
    • (2000) J Mol Biol , vol.299 , pp. 487-498
    • Fleming, P.J.1    Richards, F.M.2
  • 29
    • 0024284779 scopus 로고
    • Sequential proton NMR assignments and secondary structure of hen egg white lysozyme in solution
    • Redfield C, Dobson CM. Sequential proton NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry (US) 1988;27:122-36.
    • (1988) Biochemistry (US) , vol.27 , pp. 122-136
    • Redfield, C.1    Dobson, C.M.2
  • 30
    • 0030026989 scopus 로고    scopus 로고
    • Protein adsorption on solid surfaces
    • Hlady V, Buijs J. Protein adsorption on solid surfaces. Curr Opin Biotechnol 1996;7:72-7.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 72-77
    • Hlady, V.1    Buijs, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.