메뉴 건너뛰기




Volumn 23, Issue 10, 2012, Pages 1768-1777

Erratum to: Quantifying protein-ligand binding constants using electrospray ionization mass spectrometry: A systematic binding affinity study of a series of hydrophobically modified trypsin inhibitors (Journal of the American Society for Mass Spectrometry (2012) 23, (1768-1777) DOI: 10.1007/s13361-012-0451-6);Quantifying protein-ligand binding constants using electrospray ionization mass spectrometry: A systematic binding affinity study of a series of hydrophobically modified trypsin inhibitors

Author keywords

Binding affinity; Electrospray ionization mass spectrometry; Hydrophobic effect; Noncovalent interactions; Protein ligand complexes; Trypsin

Indexed keywords

BINDING ENERGY; CHAINS; COMPLEXATION; DISSOCIATION; HYDROPHOBICITY; IONIZATION OF GASES; IONS; LIGANDS; MASS SPECTROMETRY; PROTEINS;

EID: 84868260683     PISSN: 10440305     EISSN: 18791123     Source Type: Journal    
DOI: 10.1007/s13361-014-0907-y     Document Type: Erratum
Times cited : (40)

References (54)
  • 1
    • 33745652264 scopus 로고    scopus 로고
    • Applications of ESI-MS in drug discovery: Interrogation of noncovalent complexes
    • Hofstadler, S.A., Sannes-Lowery, K.A.: Applications of ESI-MS in drug discovery: Interrogation of noncovalent complexes. Nat. Rev. Drug Discov. 5(7), 585-595 (2006)
    • (2006) Nat. Rev. Drug Discov. , vol.5 , Issue.7 , pp. 585-595
    • Hofstadler, S.A.1    Sannes-Lowery, K.A.2
  • 2
    • 0037090377 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry
    • Daniel, J.M., Friess, S.D., Rajagopalan, S., Wendt, S., Zenobi, R.: Quantitative determination of noncovalent binding interactions using soft ionization mass spectrometry. Int. J. Mass Spectrom. 216, 1-27 (2002)
    • (2002) Int. J. Mass Spectrom. , vol.216 , pp. 1-27
    • Daniel, J.M.1    Friess, S.D.2    Rajagopalan, S.3    Wendt, S.4    Zenobi, R.5
  • 3
    • 3543008337 scopus 로고    scopus 로고
    • Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry
    • Tjernberg, A., Carno, S., Oliv, F., Benkestock, K., Edlund, P.O., Griffiths, W.J., Hallen, D.: Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry. Anal. Chem. 76, 4325-4331 (2004)
    • (2004) Anal. Chem. , vol.76 , pp. 4325-4331
    • Tjernberg, A.1    Carno, S.2    Oliv, F.3    Benkestock, K.4    Edlund, P.O.5    Griffiths, W.J.6    Hallen, D.7
  • 4
    • 44649201041 scopus 로고    scopus 로고
    • Binding constant determination of high-affinity protein-ligand complexes by electrospray ionization mass spectrometry and ligand competition
    • Wortmann, A., Jecklin, M.C., Touboul, D., Badertscher, M., Zenobi, R.: Binding constant determination of high-affinity protein-ligand complexes by electrospray ionization mass spectrometry and ligand competition. J. Mass Spectrom. 43, 600-608 (2007)
    • (2007) J. Mass Spectrom. , vol.43 , pp. 600-608
    • Wortmann, A.1    Jecklin, M.C.2    Touboul, D.3    Badertscher, M.4    Zenobi, R.5
  • 6
    • 32444451730 scopus 로고    scopus 로고
    • Applications of mass spectrometry in early stages of target based drug discovery
    • Deng, G.J., Sanyal, G.: Applications of mass spectrometry in early stages of target based drug discovery. J. Pharm. Biomed. Anal. 40, 528-538 (2006)
    • (2006) J. Pharm. Biomed. Anal. , vol.40 , pp. 528-538
    • Deng, G.J.1    Sanyal, G.2
  • 7
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J.A.: Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16, 1-23 (1997)
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 8
    • 4644327652 scopus 로고    scopus 로고
    • Native protein mass spectrometry: From intact oligomers to functional machineries
    • Van den Heuvel, R.H., Heck, A.J.: Native protein mass spectrometry: From intact oligomers to functional machineries. Curr. Opin. Chem. Biol. 8, 519-526 (2004)
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 519-526
    • Van Den Heuvel, R.H.1    Heck, A.J.2
  • 9
    • 0038293125 scopus 로고    scopus 로고
    • Quantification of protein-ligand interactions by mass spectrometry, titration, and H/D exchange: PLIMSTEX
    • 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)
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5252-5253
    • Zhu, M.M.1    Rempel, D.L.2    Du, Z.3    Gross, M.L.4
  • 10
    • 11844258744 scopus 로고    scopus 로고
    • A novel mass spectrometric method for the quantification of protein-ligand interactions in solution
    • Zhu, M.M., Chitta, R., Gross, M.L.: A novel mass spectrometric method for the quantification of protein-ligand interactions in solution. Int. J. Mass Spectrom 240, 213-240 (2005)
    • (2005) Int. J. Mass Spectrom , vol.240 , pp. 213-240
    • Zhu, M.M.1    Chitta, R.2    Gross, M.L.3
  • 13
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace, C., Shirley, B., McNutt, M., Gajiwala, K.: Forces contributing to the conformational stability of proteins. FASEB J. 10(1), 75-83 (1996)
    • (1996) FASEB J. , vol.10 , Issue.1 , pp. 75-83
    • Pace, C.1    Shirley, B.2    McNutt, M.3    Gajiwala, K.4
  • 14
    • 38849196324 scopus 로고    scopus 로고
    • Water as an active constituent in cell biology
    • Ball, P.: Water as an active constituent in cell biology. Chem. Rev. 108 (1), 74-108 (2008)
    • (2008) Chem. Rev. , vol.108 , Issue.1 , pp. 74-108
    • Ball, P.1
  • 15
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W.: Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14, 1-63 (1959)
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 16
    • 0001928266 scopus 로고    scopus 로고
    • Collision-induced dissociation of noncovalent complexes between vancomycin antibiotics and peptide ligand stereoisomers: Evidence for molecular recognition in the gas phase
    • Jørgensen, T.J.D., Delforge, D., Remacle, J., Bojesen, G., Roepstorff, P.: Collision-induced dissociation of noncovalent complexes between vancomycin antibiotics and peptide ligand stereoisomers: Evidence for molecular recognition in the gas phase. Int. J. Mass Spectrom. 188, 63-85 (1999)
    • (1999) Int. J. Mass Spectrom. , vol.188 , pp. 63-85
    • Jørgensen, T.J.D.1    Delforge, D.2    Remacle, J.3    Bojesen, G.4    Roepstorff, P.5
  • 17
    • 0031018564 scopus 로고    scopus 로고
    • Carbonic anhydrase-inhibitor binding: From solution to the gas phase
    • Wu, Q.Y.: Carbonic anhydrase-inhibitor binding: From solution to the gas phase. J. Am. Chem. Soc. 119, 1157-1158 (1997)
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1157-1158
    • Wu, Q.Y.1
  • 18
    • 35648942251 scopus 로고    scopus 로고
    • Quantitative determination of lysozymeligand binding in the solution and gas phases by electrospray ionisation mass spectrometry
    • Veros, C.T., Oldham, N.J.: Quantitative determination of lysozymeligand binding in the solution and gas phases by electrospray ionisation mass spectrometry. Rapid Commun. Mass Spectrom. 21(21), 3505-3510 (2007)
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , Issue.21 , pp. 3505-3510
    • Veros, C.T.1    Oldham, N.J.2
  • 20
    • 79960007398 scopus 로고    scopus 로고
    • What happens to hydrophobic interactions during transfer from the solution to the gas phase? The case of electrospray-based soft ionization methods
    • Barylyuk, K., Balabin, R., Grönstein, D., Kikkeri, R., Frankevich, V., Seeberger, P., Zenobi, R.: What happens to hydrophobic interactions during transfer from the solution to the gas phase? The case of electrospray-based soft ionization methods. J. Am. Soc. Mass Spectrom. 22(7), 1167-1177 (2011)
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , Issue.7 , pp. 1167-1177
    • Barylyuk, K.1    Balabin, R.2    Grönstein, D.3    Kikkeri, R.4    Frankevich, V.5    Seeberger, P.6    Zenobi, R.7
  • 21
    • 79952511159 scopus 로고    scopus 로고
    • Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
    • Liu, L., Kitova, E., Klassen, J.: Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 22(2), 310-318 (2011)
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , Issue.2 , pp. 310-318
    • Liu, L.1    Kitova, E.2    Klassen, J.3
  • 22
    • 77958179943 scopus 로고    scopus 로고
    • Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
    • El-Hawiet, A., Kitova, E., Liu, L., Klassen, J.: Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 21(11), 1893-1899 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , Issue.11 , pp. 1893-1899
    • El-Hawiet, A.1    Kitova, E.2    Liu, L.3    Klassen, J.4
  • 23
    • 70450173054 scopus 로고    scopus 로고
    • Hydrophobic protein-ligand interactions preserved in the gas phase
    • Liu, L., Bagal, D., Kitova, E.N., Schnier, P.D., Klassen, J.S.: Hydrophobic protein-ligand interactions preserved in the gas phase. J. Am. Chem. Soc. 131(44), 15980-15981 (2009)
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.44 , pp. 15980-15981
    • Liu, L.1    Bagal, D.2    Kitova, E.N.3    Schnier, P.D.4    Klassen, J.S.5
  • 24
    • 78650261675 scopus 로고    scopus 로고
    • Evidence that water can reduce the kinetic stability of protein-hydrophobic ligand interactions
    • Liu, L., Michelsen, K., Kitova, E.N., Schnier, P.D., Klassen, J.S.: Evidence that water can reduce the kinetic stability of protein-hydrophobic ligand interactions. J. Am. Chem. Soc. 132(50), 17658-17660 (2010)
    • (2010) J. Am. Chem. Soc. , vol.132 , Issue.50 , pp. 17658-17660
    • Liu, L.1    Michelsen, K.2    Kitova, E.N.3    Schnier, P.D.4    Klassen, J.S.5
  • 25
    • 74249106137 scopus 로고    scopus 로고
    • Probing the hydrophobic effect of noncovalent complexes by mass spectrometry
    • Bich, C., Baer, S., Jecklin, M., Zenobi, R.: Probing the hydrophobic effect of noncovalent complexes by mass spectrometry. J. Am. Soc. Mass Spectrom. 21(2), 286-289 (2010)
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , Issue.2 , pp. 286-289
    • Bich, C.1    Baer, S.2    Jecklin, M.3    Zenobi, R.4
  • 26
    • 33846194221 scopus 로고    scopus 로고
    • Method for stabilizing proteinligand complexes in nanoelectrospray ionization mass spectrometry
    • Sun, J.X., Kitova, E.N., Klassen, J.S.: Method for stabilizing proteinligand complexes in nanoelectrospray ionization mass spectrometry. Anal. Chem. 79(2), 416-425 (2007)
    • (2007) Anal. Chem. , vol.79 , Issue.2 , pp. 416-425
    • Sun, J.X.1    Kitova, E.N.2    Klassen, J.S.3
  • 27
    • 70349126310 scopus 로고    scopus 로고
    • Gas phase stabilization of noncovalent protein complexes formed by electrospray ionization
    • Bagal, D., Kitova, E.N., Liu, L., El-Hawiet, A., Schnier, P.D., Klassen, J.S.: Gas phase stabilization of noncovalent protein complexes formed by electrospray ionization. Anal. Chem. 81(18), 7801-7806 (2009)
    • (2009) Anal. Chem. , vol.81 , Issue.18 , pp. 7801-7806
    • Bagal, D.1    Kitova, E.N.2    Liu, L.3    El-Hawiet, A.4    Schnier, P.D.5    Klassen, J.S.6
  • 28
    • 0029794153 scopus 로고    scopus 로고
    • Probing the nature of noncovalent interactions by mass spectrometry. A study of protein-coA ligand binding and assembly
    • Robinson, C.V.: Probing the nature of noncovalent interactions by mass spectrometry. A study of protein-coA ligand binding and assembly. J. Am. Chem. Soc. 118, 8646-8653 (1996)
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8646-8653
    • Robinson, C.V.1
  • 29
    • 10044271179 scopus 로고    scopus 로고
    • Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements
    • Clark, S.M., Konermann, L.: Determination of ligand-protein dissociation constants by electrospray mass spectrometry-based diffusion measurements. Anal. Chem. 76(23), 7077-7083 (2004)
    • (2004) Anal. Chem. , vol.76 , Issue.23 , pp. 7077-7083
    • Clark, S.M.1    Konermann, L.2
  • 30
    • 34247572309 scopus 로고    scopus 로고
    • Estrogen receptor-ligand complexes measured by chip-based nanoelectrospray mass spectrometry: An approach for the screening of endocrine disruptors
    • Bovet, C., Wortmann, A., Eiler, S., Granger, F., Ruff, M., Gerrits, B., Moras, D., Zenobi, R.: Estrogen receptor-ligand complexes measured by chip-based nanoelectrospray mass spectrometry: an approach for the screening of endocrine disruptors. Protein Sci. 16(5), 938-946 (2007)
    • (2007) Protein Sci. , vol.16 , Issue.5 , pp. 938-946
    • Bovet, C.1    Wortmann, A.2    Eiler, S.3    Granger, F.4    Ruff, M.5    Gerrits, B.6    Moras, D.7    Zenobi, R.8
  • 31
    • 40249115327 scopus 로고    scopus 로고
    • Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? A comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry
    • Jecklin, M., Touboul, D., Bovet, C., Wortmann, A., Zenobi, R.: Which electrospray-based ionization method best reflects protein-ligand interactions found in solution? A comparison of ESI, nanoESI, and ESSI for the determination of dissociation constants with mass spectrometry. J. Am. Soc. Mass Spectrom. 19(3), 332-343 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , Issue.3 , pp. 332-343
    • Jecklin, M.1    Touboul, D.2    Bovet, C.3    Wortmann, A.4    Zenobi, R.5
  • 32
    • 67650264161 scopus 로고    scopus 로고
    • Label-free determination of protein-ligand binding constants using mass spectrometry and validation using surface plasmon resonance and isothermal titration calorimetry
    • Jecklin, M.C., Schauer, S., Dumelin, C.E., Zenobi, R.: Label-free determination of protein-ligand binding constants using mass spectrometry and validation using surface plasmon resonance and isothermal titration calorimetry. J. Mol. Rec. 22(4), 319-329 (2009)
    • (2009) J. Mol. Rec. , vol.22 , Issue.4 , pp. 319-329
    • Jecklin, M.C.1    Schauer, S.2    Dumelin, C.E.3    Zenobi, R.4
  • 33
    • 0032532125 scopus 로고    scopus 로고
    • Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry
    • Jørgensen, T.J.D., Roepstorff, P.: Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry. Anal. Chem. 70, 4427-4432 (1998)
    • (1998) Anal. Chem. , vol.70 , pp. 4427-4432
    • Jørgensen, T.J.D.1    Roepstorff, P.2
  • 34
    • 0042820036 scopus 로고    scopus 로고
    • Direct mass spectrometric determination of the stoichiometry and binding affinity of the complexes between nucleocapsid protein and RNA stem-loop hairpins of the HIV-1 psi-recognition element
    • Hagan, N., Fabris, D.: Direct mass spectrometric determination of the stoichiometry and binding affinity of the complexes between nucleocapsid protein and RNA stem-loop hairpins of the HIV-1 Psi-recognition element. Biochemistry 42, 10736-10745 (2003)
    • (2003) Biochemistry , vol.42 , pp. 10736-10745
    • Hagan, N.1    Fabris, D.2
  • 35
    • 0034824115 scopus 로고    scopus 로고
    • Thermodynamic analysis of binding of p-substituted benzamidines to trypsin
    • Talhout, R., Engberts, J.B.F.N.: Thermodynamic analysis of binding of p-substituted benzamidines to trypsin. Eur. J. Biochem. 268, 1554-1560 (2001)
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1554-1560
    • Talhout, R.1    Engberts, J.B.F.N.2
  • 36
    • 38549103718 scopus 로고    scopus 로고
    • Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions
    • Wang, Y., Luo, W., Reiser, G.: Trypsin and trypsin-like proteases in the brain: Proteolysis and cellular functions. Cell. Mol. Life Sci. 65(2), 237-252 (2008)
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.2 , pp. 237-252
    • Wang, Y.1    Luo, W.2    Reiser, G.3
  • 37
    • 0033451527 scopus 로고    scopus 로고
    • Binding of aldose reductase inhibitors: Correlation of crystallographic and mass spectrometric studies
    • Rogniaux, H.: Binding of aldose reductase inhibitors: Correlation of crystallographic and mass spectrometric studies. J. Am. Soc. Mass Spectrom. 10, 635-647 (1999)
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 635-647
    • Rogniaux, H.1
  • 38
    • 0029347588 scopus 로고
    • Using electrospray ionization FTICR mass spectrometry to study competitive binding of inhibitors to carbonic anhydrase
    • Cheng, X.: Using electrospray ionization FTICR mass spectrometry to study competitive binding of inhibitors to carbonic anhydrase. J. Am. Chem. Soc. 117, 8859-8860 (1995)
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8859-8860
    • Cheng, X.1
  • 40
    • 48349127727 scopus 로고    scopus 로고
    • Mass spectrometry of protein-ligand complexes: Enhanced gas-phase stability of ribonuclease-nucleotide complexes
    • Yin, S., Xie, Y., Loo, J.A.: Mass spectrometry of protein-ligand complexes: enhanced gas-phase stability of ribonuclease-nucleotide complexes. J. Am. Soc. Mass Spectrom. 19, 1199-1208 (2008)
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1199-1208
    • Yin, S.1    Xie, Y.2    Loo, J.A.3
  • 42
    • 0027997748 scopus 로고
    • Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing
    • Little, D.P., Speir, J.P., Senko, M.W., O'Connor, P.B., McLafferty, F.W.: Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing. Anal. Chem. 66, 2809-2815 (1994)
    • (1994) Anal. Chem. , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Connor, P.B.4    McLafferty, F.W.5
  • 43
    • 0029085077 scopus 로고
    • Characterization of leucine zipper complexes by electrospray ionization mass spectrometry
    • Wendt, H., Durr, E., Thomas, R.M., Przybylski, M., Bosshard, H.R.: Characterization of leucine zipper complexes by electrospray ionization mass spectrometry. Protein Sci. 4, 1563-1570 (1995)
    • (1995) Protein Sci. , vol.4 , pp. 1563-1570
    • Wendt, H.1    Durr, E.2    Thomas, R.M.3    Przybylski, M.4    Bosshard, H.R.5
  • 44
    • 0034839464 scopus 로고    scopus 로고
    • Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry
    • Nesatyy, V.J.: Gas-phase binding of non-covalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 36, 950-959 (2001)
    • (2001) J. Mass Spectrom. , vol.36 , pp. 950-959
    • Nesatyy, V.J.1
  • 46
    • 79952761054 scopus 로고    scopus 로고
    • A quantitative perspective on hydrophobic interactions in the gas-phase
    • Sharon, M., Robinson, C.V.: A quantitative perspective on hydrophobic interactions in the gas-phase. Curr. Proteom. 8(1), 47-58 (2011)
    • (2011) Curr. Proteom. , vol.8 , Issue.1 , pp. 47-58
    • Sharon, M.1    Robinson, C.V.2
  • 47
    • 0024328497 scopus 로고
    • Synthetic inhibitors of bovine factor xa and thrombin comparison of their anticoagulant efficiency
    • Stürzebecher, J., Stürzebecher, U., Vieweg, H., Wagner, G., Hauptmann, J., Markwardt, F.: Synthetic inhibitors of bovine factor Xa and thrombin comparison of their anticoagulant efficiency. Thromb. Res. 54(3), 245-252 (1989)
    • (1989) Thromb. Res. , vol.54 , Issue.3 , pp. 245-252
    • Stürzebecher, J.1    Stürzebecher, U.2    Vieweg, H.3    Wagner, G.4    Hauptmann, J.5    Markwardt, F.6
  • 48
    • 0032730993 scopus 로고    scopus 로고
    • Non-boltzmann thermodynamic integration (NBTI) for macromolecular systems: Relative free energy of binding of trypsin to benzamidine and benzylamine
    • Ota, N., Stroupe, C., Ferreira-da-Silva, J.M.S., Shah, S.A., Mares-Guia, M., Brunger, A.T.: Non-Boltzmann thermodynamic integration (NBTI) for macromolecular systems: Relative free energy of binding of trypsin to benzamidine and benzylamine. Proteins 37(4), 641-653 (1999)
    • (1999) Proteins , vol.37 , Issue.4 , pp. 641-653
    • Ota, N.1    Stroupe, C.2    Ferreira-Da-Silva, J.M.S.3    Shah, S.A.4    Mares-Guia, M.5    Brunger, A.T.6
  • 49
    • 0035906508 scopus 로고    scopus 로고
    • Noncovalent interactions between tetrazole and an N, N'-diethyl- substituted benzamidine
    • Peters, L., Frohlich, R., Boyd, A.S.F., Kraft, A.: Noncovalent interactions between tetrazole and an N, N'-diethyl-substituted benzamidine. J. Org. Chem. 66, 3291-3298 (2001)
    • (2001) J. Org. Chem. , vol.66 , pp. 3291-3298
    • Peters, L.1    Frohlich, R.2    Boyd, A.S.F.3    Kraft, A.4
  • 50
    • 78751580378 scopus 로고    scopus 로고
    • Congeneric but still distinct: How closely related trypsin ligands exhibit different thermodynamic and structural properties
    • Brandt, T., Holzmann, N., Muley, L., Khayat, M., Wegscheid-Gerlach, C., Baum, B., Heine, A., Hangauer, D., Klebe, G.: Congeneric but still distinct: How closely related trypsin ligands exhibit different thermodynamic and structural properties. J. Mol. Biol. 405(5), 1170-1187 (2011)
    • (2011) J. Mol. Biol. , vol.405 , Issue.5 , pp. 1170-1187
    • Brandt, T.1    Holzmann, N.2    Muley, L.3    Khayat, M.4    Wegscheid-Gerlach, C.5    Baum, B.6    Heine, A.7    Hangauer, D.8    Klebe, G.9
  • 51
    • 41849107110 scopus 로고    scopus 로고
    • Understanding binding selectivity toward trypsin and factor xa: The role of aromatic interactions
    • Di Fenza, A., Heine, A., Koert, U., Klebe, G.: Understanding binding selectivity toward trypsin and factor Xa: the role of aromatic interactions. ChemMedChem 2(3), 297-308 (2007)
    • (2007) ChemMedChem , vol.2 , Issue.3 , pp. 297-308
    • Di Fenza, A.1    Heine, A.2    Koert, U.3    Klebe, G.4
  • 52
    • 85006477697 scopus 로고    scopus 로고
    • Native mass spectrometry as a tool in structural biology
    • Lorenzen, K., Duijn, E.V.: Native mass spectrometry as a tool in structural biology. Curr. Protoc. Protein Sci. 62, 17.12.1-17.12.17 (2010)
    • (2010) Curr. Protoc. Protein Sci. , vol.62 , pp. 17121-171217
    • Lorenzen, K.1    Duijn, E.V.2
  • 53
    • 0032366914 scopus 로고    scopus 로고
    • Evaluated gas phase basicities and proton affinities of molecules: An update
    • Hunter, E.P.L., Lias, S.G.: Evaluated gas phase basicities and proton affinities of molecules: An update. J. Phys. Chem. Ref. Data 27(3), 413-656 (1998)
    • (1998) J. Phys. Chem. Ref. Data , vol.27 , Issue.3 , pp. 413-656
    • Hunter, E.P.L.1    Lias, S.G.2
  • 54
    • 0035561175 scopus 로고    scopus 로고
    • Electrochemical processes in a wire-in-a-capillary bulk-loaded, nano-electrospray emitter
    • Van Berkel, G.J., Asano, K.G., Schnier, P.D.: Electrochemical processes in a wire-in-a-capillary bulk-loaded, nano-electrospray emitter. J. Am. Soc. Mass Spectrom. 12(7), 853-862 (2001)
    • (2001) J. Am. Soc. Mass Spectrom. , vol.12 , Issue.7 , pp. 853-862
    • Van Berkel, G.J.1    Asano, K.G.2    Schnier, P.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.