메뉴 건너뛰기




Volumn 23, Issue 1, 2012, Pages 30-42

Probing protein surface with a solvent mimetic carbene coupled to detection by mass spectrometry

Author keywords

Accessible surface area; Diazirine; Methylene carbene; Photochemical probe; Protein conformation

Indexed keywords

ACCESSIBLE SURFACE AREAS; AMINO ACID SEQUENCE; CARBENES; CHEMICAL NATURE; COMPLEX FORMATIONS; DIAZIRINE; ELECTROSPRAY MASS SPECTROMETRY; HIGH RESOLUTION; KEY PARAMETERS; LIGAND BINDING; MS/MS ANALYSIS; NON-NATIVE STATE; POLYPEPTIDE CHAIN; PROTEIN CONFORMATION; PROTEIN SCIENCE; PROTEIN SURFACE; SOLVENT ACCESSIBILITY; SPECTROMETRY TECHNIQUE; TARGET SITES;

EID: 84856179597     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-011-0266-x     Document Type: Article
Times cited : (11)

References (57)
  • 3
    • 0004260243 scopus 로고
    • T.E. Creighton (eds). W. H. Freeman and Company New York
    • Creighton, T.E. (ed.): Protein Folding. W. H. Freeman and Company, New York (1992)
    • (1992) Protein Folding
  • 4
    • 0004245772 scopus 로고
    • R.H. Pain (eds). IRL Press at Oxford University Press Oxford, UK
    • Pain, R.H. (ed.): Mechanisms of Protein Folding. IRL Press at Oxford University Press, Oxford, UK (1994)
    • (1994) Mechanisms of Protein Folding
  • 5
    • 0017429069 scopus 로고
    • Areas, Volumes, Packing, and Protein Structure
    • 10.1146/annurev.bb.06.060177.001055 1:CAS:528:DyaE2sXks1CisrY%3D
    • Richards, F.M.: Areas, Volumes, Packing, and Protein Structure. Annu. Rev. Biophys. Bioeng. 6, 151-176 (1977)
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 6
    • 0034493026 scopus 로고    scopus 로고
    • Methylene as a possible universal footprinting reagent that will include hydrophobic surface areas: Overview and feasibility: Properties of diazirine as a precursor
    • Richards, F.M., Lamed, R., Wynn, R., Patel, D., Olack, G.: Methylene as a Possible Universal Footprinting Reagent that will Include Hydrophobic Surface Areas. Overview and Feasibility: Properties of Diazirine as a Precursor. Protein Sci. 9, 2506-2517 (2000) (Pubitemid 32105733)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2506-2517
    • Richards, F.M.1    Lamed, R.2    Wynn, R.3    Patel, D.4    Olack, G.5
  • 7
    • 0025360593 scopus 로고
    • Heat capacity of proteins. I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
    • DOI 10.1016/S0022-2836(05)80197-4
    • Makhatadze, G.I., Privalov, P.L.: Heat Capacity of Proteins. I. Partial Molar Heat Capacity of Individual Amino Acid Residues in Aqueous Solution: Hydration Effect. J. Mol. Biol. 213, 375-384 (1990) (Pubitemid 20176546)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.2 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 8
    • 0025287103 scopus 로고
    • Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects
    • DOI 10.1016/S0022-2836(05)80198-6
    • Privalov, P.L., Makhatadze, G.I.: Heat Capacity of Proteins. II. Partial Molar Heat Capacity of the Unfolded Polypeptide Chain of Proteins: Protein Unfolding Effects. J. Mol. Biol. 213, 385-291 (1990) (Pubitemid 20176547)
    • (1990) Journal of Molecular Biology , vol.213 , Issue.2 , pp. 385-391
    • Privalov, P.L.1    Makahatadze, G.I.2
  • 9
    • 0025906146 scopus 로고
    • Contribution to the Thermodynamics of Protein Folding from the Reduction in Water-Accessible Nonpolar Surface Area
    • 10.1021/bi00231a019 1:CAS:528:DyaK3MXhvVWltb8%3D
    • Livingstone, J.R., Spolar, R.S., Record Jr., M.T.: Contribution to the Thermodynamics of Protein Folding from the Reduction in Water-Accessible Nonpolar Surface Area. Biochemistry 30, 4237-4244 (1991)
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record Jr., M.T.3
  • 11
    • 0028820703 scopus 로고
    • Denaturant m Values and Heat Capacity Changes: Relation to Changes in Accessible Surface Areas of Protein Unfolding
    • 10.1002/pro.5560041020 1:CAS:528:DyaK2MXoslygt7s%3D
    • Myers, J.K., Pace, C.N., Scholtz, J.M.: Denaturant m Values and Heat Capacity Changes: Relation to Changes in Accessible Surface Areas of Protein Unfolding. Protein Sci. 4, 2138-2148 (1995)
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 12
    • 33845923182 scopus 로고    scopus 로고
    • BPPred: A Web-based computational tool for predicting biophysical parameters of proteins
    • DOI 10.1110/ps.062383807
    • Geierhaas, C.D., Nickson, A.A., Lindorff-Larsen, K., Clarke, J., Vendruscolo, M.: BPPred: A Web-Based Computational Tool for Predicting Biophysical Parameters of Proteins. Protein Sci. 16, 125-134 (2007) (Pubitemid 46036505)
    • (2007) Protein Science , vol.16 , Issue.1 , pp. 125-134
    • Geierhaas, C.D.1    Nickson, A.A.2    Lindorff-Larsen, K.3    Clarke, J.4    Vendruscolo, M.5
  • 13
    • 69849100869 scopus 로고    scopus 로고
    • Probing Protein Structure by Amino Acid-Specific Covalent Labeling and Mass Spectrometry
    • 10.1002/mas.20203 1:CAS:528:DC%2BD1MXhtFaisbzO
    • Mendoza, V.L., Vachet, R.W.: Probing Protein Structure by Amino Acid-Specific Covalent Labeling and Mass Spectrometry. Mass Spectrom Rev. 28, 785-815 (2009)
    • (2009) Mass Spectrom Rev. , vol.28 , pp. 785-815
    • Mendoza, V.L.1    Vachet, R.W.2
  • 14
    • 65549094060 scopus 로고    scopus 로고
    • Painting Proteins with Covalent Labels: What's in the Picture?
    • 10.1016/j.jasms.2009.02.006
    • Fitzgerald, M.C., West, G.M.: Painting Proteins with Covalent Labels: What's in the Picture? J. Am. Soc. Mass Spectrom. 20, 1193-1206 (2009)
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1193-1206
    • Fitzgerald, M.C.1    West, G.M.2
  • 15
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen Exchange and Mass Spectrometry: A Historical Perspective
    • DOI 10.1016/j.jasms.2006.06.006, PII S1044030506005514
    • Englander, S.W.: Hydrogen Exchange and Mass Spectrometry: A Historical Perspective. J. Am. Soc. Mass Spectrom. 17, 1481-1489 (2006) (Pubitemid 44635273)
    • (2006) Journal of the American Society for Mass Spectrometry , vol.17 , Issue.11 , pp. 1481-1489
    • Englander, S.W.1
  • 16
    • 42449151176 scopus 로고    scopus 로고
    • Protein folding and misfolding: Mechanism and principles
    • DOI 10.1017/S0033583508004654, PII S0033583508004654
    • Englander, S.W., Mayne, L., Krishna, M.M.: Protein Folding and Misfolding: Mechanism and Principles. Q Rev. Biophys. 40, 287-326 (2007) (Pubitemid 351569384)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.4 , pp. 287-326
    • Englander, S.W.1    Mayne, L.2    Krishna, M.M.G.3
  • 17
    • 0038293125 scopus 로고    scopus 로고
    • Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX
    • DOI 10.1021/ja029460d
    • Zhu, M.M., Rempel, D.L., Du, Z., Gross, M.L.: Quantification of Protein-Ligand Interactions by Mass Spectrometry, Titration, and H/D Exchange: PLIMSTEX. J. Am. Chem. Soc. 125, 5252-5253 (2003) (Pubitemid 36582715)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.18 , pp. 5252-5253
    • Zhu, M.M.1    Rempel, D.L.2    Du, Z.3    Gross, M.L.4
  • 18
    • 0022382116 scopus 로고
    • Iron(II) EDTA used to measure the helical twist along any DNA molecule
    • Tullius, T.D., Dombroski, B.A.: Iron (II) EDTA Used to Measure the Helical Twist Along Any DNA Molecule. Science 230, 679-681 (1985) (Pubitemid 16190964)
    • (1985) Science , vol.230 , Issue.4726 , pp. 679-681
    • Tullius, T.D.1    Dombroski, B.A.2
  • 19
    • 70449661023 scopus 로고
    • Hydroxyl Radical Footprinting: A High Resolution Method for Mapping Protein-DNA Contacts
    • R. Wu L. Grossman K. Moldave (eds). Academic Press San Diego, CA
    • Tullius, T.D., Dombroski, B.A., Churchill, M.E.A., Kam, L.: Hydroxyl Radical Footprinting: A High Resolution Method for Mapping Protein-DNA Contacts. In: Wu, R., Grossman, L., Moldave, K. (eds.) Recombinant DNA Methodology. Academic Press, San Diego, CA (1989)
    • (1989) Recombinant DNA Methodology
    • Tullius, T.D.1    Dombroski, B.A.2    Churchill, M.E.A.3    Kam, L.4
  • 20
    • 44949172720 scopus 로고    scopus 로고
    • Footprinting protein - DNA complexes using the hydroxyl radical
    • DOI 10.1038/nprot.2008.72, PII NPROT.2008.72
    • Jain, S.S., Tullius, T.D.: Footprinting Protein-DNA Complexes Using the Hydroxyl Radical. Nat. Protoc. 3, 1092-1100 (2008) (Pubitemid 351818696)
    • (2008) Nature Protocols , vol.3 , Issue.6 , pp. 1092-1100
    • Jain, S.S.1    Tullius, T.D.2
  • 21
    • 0026766292 scopus 로고
    • Conformation-Dependent Cleavage of Staphylococcal Nuclease with a Disulfide-Linked Iron Chelate
    • 10.1073/pnas.89.14.6383 1:CAS:528:DyaK38Xls1Oju74%3D
    • Ermacora, M.R., Delfino, J.M., Cuenoud, B., Schepartz, A., Fox, R.O.: Conformation-Dependent Cleavage of Staphylococcal Nuclease with a Disulfide-Linked Iron Chelate. Proc. Natl. Acad. Sci. U.S.A. 89, 6383-6387 (1992)
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 6383-6387
    • Ermacora, M.R.1    Delfino, J.M.2    Cuenoud, B.3    Schepartz, A.4    Fox, R.O.5
  • 22
    • 0028096754 scopus 로고
    • Mapping staphylococcal nuclease conformation using an EDTA-Fe derivative attached to genetically engineered cysteine residues
    • DOI 10.1021/bi00250a013
    • Ermacora, M.R., Ledman, D.W., Hellinga, H.W., Hsu, G.W., Fox, R.O.: Mapping Staphylococcal Nuclease Conformation Using an EDTA-Fe Derivative Attached to Genetically Engineered Cysteine Residues. Biochemistry 33, 13625-13641 (1994) (Pubitemid 24381923)
    • (1994) Biochemistry , vol.33 , Issue.46 , pp. 13625-13641
    • Ermacora, M.R.1    Ledman, D.W.2    Hellinga, H.W.3    Hsu, G.W.4    Fox, R.O.5
  • 23
    • 0033568535 scopus 로고    scopus 로고
    • Millisecond radiolytic modification of peptides by synchrotron X-rays identified by mass spectrometry
    • DOI 10.1021/ac990500e
    • Maleknia, S.D., Brenowitz, M., Chance, M.R.: Millisecond Radiolytic Modification of Peptides by Synchrotron X-Rays Identified by Mass Spectrometry. Anal. Chem. 71, 3965-3973 (1999) (Pubitemid 29439760)
    • (1999) Analytical Chemistry , vol.71 , Issue.18 , pp. 3965-3973
    • Maleknia, S.D.1    Brenowitz, M.2    Chance, M.R.3
  • 24
    • 0035865266 scopus 로고    scopus 로고
    • Determination of macromolecular folding and structure by synchrotron X-ray radiolysis techniques
    • DOI 10.1006/abio.2000.4910
    • Maleknia, S.D., Ralston, C.Y., Brenowitz, M.D., Downard, K.M., Chance, M.R.: Determination of Macromolecular Folding and Structure by Synchrotron X-Ray Radiolysis Techniques. Anal. Biochem. 289, 103-115 (2001) (Pubitemid 32173657)
    • (2001) Analytical Biochemistry , vol.289 , Issue.2 , pp. 103-115
    • Maleknia, S.D.1    Ralston, C.Y.2    Brenowitz, M.D.3    Downard, K.M.4    Chance, M.R.5
  • 25
    • 0035719748 scopus 로고    scopus 로고
    • Unfolding of apomyoglobin helices by synchrotron radiolysis and mass spectrometry
    • DOI 10.1046/j.0014-2956.2001.02492.x
    • Maleknia, S.D., Downard, K.M.: Unfolding of Apomyoglobin Helices by Synchrotron Radiolysis and Mass Spectrometry. Eur. J. Biochem. 268, 5578-5588 (2001) (Pubitemid 34183323)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.21 , pp. 5578-5588
    • Maleknia, S.D.1    Downard, K.M.2
  • 26
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • DOI 10.1146/annurev.biophys.35.040405.102050
    • Takamoto, K., Chance, M.R.: Radiolytic Protein Footprinting with Mass Spectrometry to Probe the Structure of Macromolecular Complexes. Annu. Rev. Biophys. Biomol. Struct. 35, 251-276 (2006) (Pubitemid 43877378)
    • (2006) Annual Review of Biophysics and Biomolecular Structure , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 27
  • 28
    • 68849107091 scopus 로고    scopus 로고
    • Fast Photochemical Oxidation of Protein Footprints Faster than Protein Unfolding
    • 10.1021/ac901054w 1:CAS:528:DC%2BD1MXovFWltr0%3D
    • Gau, B.C., Sharp, J.S., Rempel, D.L., Gross, M.L.: Fast Photochemical Oxidation of Protein Footprints Faster than Protein Unfolding. Anal. Chem. 81, 6563-6571 (2009)
    • (2009) Anal. Chem. , vol.81 , pp. 6563-6571
    • Gau, B.C.1    Sharp, J.S.2    Rempel, D.L.3    Gross, M.L.4
  • 31
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • Brunner, J.: New Photolabeling and Crosslinking Methods. Annu. Rev. Biochem. 62, 483-514 (1993) (Pubitemid 23237879)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 483-514
    • Brunner, J.1
  • 32
    • 0001616947 scopus 로고
    • Design, Synthesis, and Properties of a Photoactivatable Membrane-Spanning Phospholipidic Probe
    • 10.1021/ja00062a009 1:CAS:528:DyaK3sXkvFSltrk%3D
    • Delfino, J.M., Schreiber, S.L., Richards, F.M.: Design, Synthesis, and Properties of a Photoactivatable Membrane-Spanning Phospholipidic Probe. J. Am. Chem. Soc. 115, 3458-3474 (1993)
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3458-3474
    • Delfino, J.M.1    Schreiber, S.L.2    Richards, F.M.3
  • 33
    • 0036106776 scopus 로고    scopus 로고
    • Probing protein conformation with a minimal photochemical reagent
    • DOI 10.1110/ps.4710102
    • Craig, P.O., Ureta, D.B., Delfino, J.M.: Probing Protein Conformation with a Minimal Photochemical Reagent. Protein Sci. 11, 1353-1366 (2002) (Pubitemid 34547207)
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1353-1366
    • Craig, P.O.1    Ureta, D.B.2    Delfino, J.M.3
  • 35
    • 0001058026 scopus 로고
    • Reactivity and Intersystem Crossing of Singlet Methylene in Solution
    • 10.1021/ja00241a030 1:CAS:528:DyaL2sXhtF2jtrs%3D
    • Turro, N.J., Cha, Y., Gould, I.R.: Reactivity and Intersystem Crossing of Singlet Methylene in Solution. J. Am. Chem. Soc. 109, 2101-2107 (1987)
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 2101-2107
    • Turro, N.J.1    Cha, Y.2    Gould, I.R.3
  • 36
    • 70449652595 scopus 로고    scopus 로고
    • Experimentally Approaching the Solvent-Accessible Surface Area of a Protein: Insights into the Acid Molten Globule of Bovine α-Lactalbumin
    • 10.1016/j.jmb.2009.09.058 1:CAS:528:DC%2BD1MXhsVKnurjM
    • Craig, P.O., Gómez, G.E., Ureta, D.B., Caramelo, J.J., Delfino, J.M.: Experimentally Approaching the Solvent-Accessible Surface Area of a Protein: Insights into the Acid Molten Globule of Bovine α-Lactalbumin. J. Mol. Biol. 394, 982-993 (2009)
    • (2009) J. Mol. Biol. , vol.394 , pp. 982-993
    • Craig, P.O.1    Gómez, G.E.2    Ureta, D.B.3    Caramelo, J.J.4    Delfino, J.M.5
  • 37
    • 37249008115 scopus 로고    scopus 로고
    • Assessing native and non-native conformational states of a protein by methylene carbene labeling: The case of Bacillus licheniformis β-lactamase
    • DOI 10.1021/bi7012867
    • Ureta, D.B., Craig, P.O., Gómez, G.E., Delfino, J.M.: Assessing Native and Non-Native Conformational States of a Protein by Methylene Carbene Labeling: The Case of Bacillus licheniformis β-lactamase. Biochemistry 46, 14567-14577 (2007) (Pubitemid 350276362)
    • (2007) Biochemistry , vol.46 , Issue.50 , pp. 14567-14577
    • Ureta, D.B.1    Craig, P.O.2    Gomez, G.E.3    Delfino, J.M.4
  • 38
    • 33645517812 scopus 로고    scopus 로고
    • Exploring Protein Interfaces with a General Photochemical Reagent
    • 10.1110/ps.051960406
    • Gómez, G.E., Cauerhff, A., Craig, P.O., Goldbaum, F.A., Delfino, J.M.: Exploring Protein Interfaces with a General Photochemical Reagent. Protein Sci. 15, 744-752 (2006)
    • (2006) Protein Sci. , vol.15 , pp. 744-752
    • Gómez, G.E.1    Cauerhff, A.2    Craig, P.O.3    Goldbaum, F.A.4    Delfino, J.M.5
  • 39
    • 1942473144 scopus 로고    scopus 로고
    • Denaturation of replication protein A reveals an alternative conformation with intact domain structure and oligonucleotide binding activity
    • DOI 10.1110/ps.04616304
    • Nuss, J.E., Alter, G.M.: Denaturation of Replication Protein A Reveals an Alternative Conformation with Intact Domain Structure and Oligonucleotide Binding Activity. Protein Sci. 13, 1365-1378 (2004) (Pubitemid 38526102)
    • (2004) Protein Science , vol.13 , Issue.5 , pp. 1365-1378
    • Nuss, J.E.1    Alter, G.M.2
  • 42
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • DOI 10.1021/bi9905819
    • Ibarra-Molero, B., Loladze, V.V., Makhatadze, G.I., Sanchez-Ruiz, J.M.: Thermal Versus Guanidine-Induced Unfolding of Ubiquitin. An Analysis in Terms of the Contributions from Charge-Charge Interactions to Protein Stability. Biochemistry 38, 8138-8149 (1999) (Pubitemid 29302387)
    • (1999) Biochemistry , vol.38 , Issue.25 , pp. 8138-8149
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4
  • 43
    • 0001501418 scopus 로고
    • Inter- and intramolecular interactions of →-lactalbumin. I. The apparent heterogeneity at acid pH
    • 10.1021/bi00896a024 1:CAS:528:DyaF2cXksVWnuro%3D
    • Kronman, M.J., Andreotti, R.E.: Inter- and intramolecular interactions of →-lactalbumin. I. The apparent heterogeneity at acid pH. Biochemistry 3, 1145-1151 (1964)
    • (1964) Biochemistry , vol.3 , pp. 1145-1151
    • Kronman, M.J.1    Andreotti, R.E.2
  • 44
    • 0010843136 scopus 로고
    • Peptides Derived from Tryptic Digestion of Egg White Lysozyme
    • 1:CAS:528:DyaF3sXkt1art7o%3D
    • Canfield, R.E.: Peptides Derived from Tryptic Digestion of Egg White Lysozyme. J. Biol. Chem. 238, 2691-2697 (1963)
    • (1963) J. Biol. Chem. , vol.238 , pp. 2691-2697
    • Canfield, R.E.1
  • 45
    • 0014409017 scopus 로고
    • Subtilisin Carlsberg. 3. Isolation and Amino Acid Composition of Chymotryptic Peptides
    • 1:CAS:528:DyaF1cXhtVaitL8%3D
    • Landon, M., Evans, W.H., Smith, E.L.: Subtilisin Carlsberg. 3. Isolation and Amino Acid Composition of Chymotryptic Peptides. J. Biol. Chem. 243, 2165-2171 (1968)
    • (1968) J. Biol. Chem. , vol.243 , pp. 2165-2171
    • Landon, M.1    Evans, W.H.2    Smith, E.L.3
  • 46
    • 0025335184 scopus 로고
    • The role of lysine-234 in β-lactamase catalysis probed by site-directed mutagenesis
    • DOI 10.1021/bi00476a022
    • Ellerby, L.M., Escobar, W.A., Fink, A.L., Mitchinson, C., Wells, J.A.: The Role of Lysine-234 in β-Lactamase Catalysis Probed by Site-Directed Mutagenesis. Biochemistry 29, 5797-5806 (1990) (Pubitemid 20192452)
    • (1990) Biochemistry , vol.29 , Issue.24 , pp. 5797-5806
    • Ellerby, L.M.1    Escobar, W.A.2    Fink, A.L.3    Mitchinson, C.4    Wells, J.A.5
  • 47
    • 77049205068 scopus 로고
    • The Terminal Groups of the Soy bean trypsin inhibitor
    • 1:CAS:528:DyaG2MXjt1OjtA%3D%3D
    • Davie, E.W., Neurath, H.: The Terminal Groups of the Soy bean trypsin inhibitor. J. Biol. Chem. 212, 507-514 (1955)
    • (1955) J. Biol. Chem. , vol.212 , pp. 507-514
    • Davie, E.W.1    Neurath, H.2
  • 48
    • 0014963344 scopus 로고
    • Comparison of Direct Spectrophotometric Methods for the Measurement of Protein Concentration
    • 1:CAS:528:DyaE3cXksFaqs7o%3D
    • Webster, G.C.: Comparison of Direct Spectrophotometric Methods for the Measurement of Protein Concentration. Biochim. Biophys. Acta 207, 371-373 (1970)
    • (1970) Biochim. Biophys. Acta , vol.207 , pp. 371-373
    • Webster, G.C.1
  • 49
    • 0018967724 scopus 로고
    • Positive cooperative binding of calcium to bovine brain calmodulin
    • DOI 10.1021/bi00557a009
    • Crouch, T.H., Klee, C.B.: Positive Cooperative Binding of Calcium to Bovine Brain Calmodulin. Biochemistry 19, 3692-3698 (1980) (Pubitemid 10023283)
    • (1980) Biochemistry , vol.19 , Issue.16 , pp. 3692-3698
    • Crouch, T.H.1    Klee, C.B.2
  • 50
    • 84981753057 scopus 로고
    • Notiz über eine einfache synthese des Cyclo-Diazomethans
    • 10.1002/cber.19640970142 1:CAS:528:DyaF2cXjvVOgug%3D%3D
    • Ohme, R., Schmitz, E.: Notiz über eine einfache synthese des Cyclo-Diazomethans. Chem. Ber. 97, 297-298 (1964)
    • (1964) Chem. Ber. , vol.97 , pp. 297-298
    • Ohme, R.1    Schmitz, E.2
  • 51
    • 0014285429 scopus 로고
    • The Covalent Structure of a Human γ G-Immunoglobulin: II. Isolation and Characterization of the Cyanogen Bromide Fragments
    • 10.1021/bi00845a046 1:CAS:528:DyaF1cXktVWgu7w%3D
    • Waxdal, M.J., Konigsberg, W.H., Henley, W.L., Edelman, G.M.: The Covalent Structure of a Human γ G-Immunoglobulin: II. Isolation and Characterization of the Cyanogen Bromide Fragments. Biochemistry 7, 1959-1966 (1968)
    • (1968) Biochemistry , vol.7 , pp. 1959-1966
    • Waxdal, M.J.1    Konigsberg, W.H.2    Henley, W.L.3    Edelman, G.M.4
  • 52
    • 0037197254 scopus 로고    scopus 로고
    • Novel computer program for fast exact calculation of accessible and molecular surface areas and average surface curvature
    • DOI 10.1002/jcc.10061
    • Tsodikov, O.V., Record Jr., M.T., Sergeev, Y.V.: A Novel Computer Program for Fast Exact Calculation of Accessible and Molecular Surface Areas and Average Surface Curvature. J. Comput. Chem. 23, 600-609 (2002) (Pubitemid 34312083)
    • (2002) Journal of Computational Chemistry , vol.23 , Issue.6 , pp. 600-609
    • Tsodikov, O.V.1    Thomas Record Jr., M.2    Sergeev, Y.V.3
  • 53
    • 0020475449 scopus 로고
    • A Simple Method for Displaying the Hydropathic Character of a Protein
    • 10.1016/0022-2836(82)90515-0 1:CAS:528:DyaL38Xks1yjtro%3D
    • Kyte, J., Doolittle, R.F.: A Simple Method for Displaying the Hydropathic Character of a Protein. J. Mol. Biol. 157, 105-132 (1982)
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 54
    • 0030759665 scopus 로고    scopus 로고
    • Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea
    • DOI 10.1021/bi970049q
    • Schwalbe, H., Fiebig, K.M., Buck, M., Jones, J.A., Grimshaw, S.B., Spencer, A., Glaser, S.J., Smith, L.J., Dobson, C.M.: Structural and Dynamic Properties of a Denatured Protein. Heteronuclear 3D NMR Experiments and Theoretical Simulations of Lysozyme in 8 M Urea. Biochemistry 36, 8977-8991 (1997) (Pubitemid 27342545)
    • (1997) Biochemistry , vol.36 , Issue.29 , pp. 8977-8991
    • Schwalbe, H.1    Fiebig, K.M.2    Buck, M.3    Jones, J.A.4    Grimshaw, S.B.5    Spencer, A.6    Glaser, S.J.7    Smith, L.J.8    Dobson, C.M.9
  • 55
    • 33744470104 scopus 로고    scopus 로고
    • Characterization of the unfolded state of bovine α-lactalbumin and comparison with unfolded states of homologous proteins
    • DOI 10.1110/ps.051974506
    • Wirmer, J., Berk, H., Ugolini, R., Redfield, C., Schwalbe, H.: Characterization of the Unfolded State of Bovine∈→∈-Lactalbumin and Comparison with Unfolded States of Homologous Proteins. Protein Sci. 15, 1397-1407 (2006) (Pubitemid 43800011)
    • (2006) Protein Science , vol.15 , Issue.6 , pp. 1397-1407
    • Wirmer, J.1    Berk, H.2    Ugolini, R.3    Redfield, C.4    Schwalbe, H.5
  • 57
    • 79954495877 scopus 로고    scopus 로고
    • Mass Spectrometry of Laser-Initiated Carbene Reactions for Protein Topographic Analysis
    • 10.1021/ac102655f 1:CAS:528:DC%2BC3MXjs1Sjtr4%3D
    • Jumper, C.C., Schriemer, D.C.: Mass Spectrometry of Laser-Initiated Carbene Reactions for Protein Topographic Analysis. Anal Chem. 83, 2913-2920 (2011)
    • (2011) Anal Chem. , vol.83 , pp. 2913-2920
    • Jumper, C.C.1    Schriemer, D.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.