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| This list includes many recent literature contributions about protein research involving hydrogen exchange and mass spectrometry. The list is by no means complete. The field is rapidly growing and new work is being added all the time. To compile the list, WE NEED YOUR HELP.
2001
2000 Engen, J.R. & Smith, D.L. (2000). Investigating the higher order structure of proteins: Hydrogen exchange, proteolytic fragmentation & mass spectrometry. In "Protein and Peptide Analysis: New Mass Spectrometric Applications" (J. Chapmann, ed.). Meth. Mol. Biol. Vol. 146. 1999 Ehring H. (1999). Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions. Anal Biochem. 267(2), 252-259. 1997 Smith, D.L., Deng, Y., and Zhang, Z. (1997). Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32, 135-146. 1996 Miranker A, Robinson C.V., Radford S.E., Dobson C.M. (1996). Investigation of protein folding by mass spectrometry. FASEB J. 10(1), 93-101.
2001 Demmers, J.A.A., van Duijn, E., Haverkamp, J., Greathouse, D.V., Koeppe 2nd, R.E., Heck, A.J.R., Killian, J.A. (2001) Interfacial positioning and stability of transmembrane peptides in lipid bilayers studied by combining hydrogen/deuterium exchange and mass spectrometry. J. Biol. Chem. 276, 34501-34508. Ghaemmaghami S, Oas TG. (2001). Quantitative protein stability measurement in vivo. Nat Struct Biol. 8(10), 879-82. Last AM, Schulman BA, Robinson CV, Redfield C. (2001). Probing Subtle Differences in the Hydrogen Exchange Behavior of Variants of the Human alpha-Lactalbumin Molten Globule Using Mass Spectrometry. J Mol Biol. 311(4), 909-19. Lorenz SA, Maziarz EP 3rd, Wood TD. (2001) Using solution phase hydrogen/deuterium (H/D) exchange to determine the origin of non-covalent complexes observed by electrospray ionization mass spectrometry: in solution or in vacuo? J Am Soc Mass Spectrom. 12(7), 795-804. Gonzalez de Peredo A, Saint-Pierre C, Latour JM, Michaud-Soret I, Forest E. (2001). Conformational changes of the ferric uptake regulation protein upon metal activation and DNA binding; first evidence of structural homologies with the diphtheria toxin repressor. J Mol Biol. 310(1), 83-91. Powell, K.D. & Fitzgerald, M.C. (2001). Measurements of Protein Stability by H/D Exchange and Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Using Picomoles of Material. Anal. Chem. 73, 3300-3304.
Chen J, Walter S, Horwich AL, Smith DL.(2001). Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nat Struct Biol. 8(8), 721-8. Wang L, Lane LC, Smith DL. (2001). Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry. Protein Sci. 10(6), 1234-43. Chang ST, Tobler SA, Fernandez EJ. (2001). Unfolding and conformational distributions during protein precipitation. Biotechnol Prog. 17(3), 583-5. Buijs J, Hagman C, Hakansson K, Richter JH, Hakansson P, Oscarsson S. (2001). Inter- and intra-molecular migration of peptide amide hydrogens during electrospray ionization. J Am Soc Mass Spectrom. 12(4), 410-9. Chen J, Smith DL. (2001). Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5. Protein Sci. 10(5), 1079-83. Hughes CA, Mandell JG, Anand GS, Stock AM, Komives EA. (2001). Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB. J Mol Biol. 307(4), 967-76. Babu KR, Moradian A, Douglas DJ. (2001). The methanol-induced conformational transitions of beta-lactoglobulin, cytochrome c, and ubiquitin at low pH: a study by electrospray ionization mass spectrometry. J Am Soc Mass Spectrom. 12(3), 317-28. Andersen MD, Shaffer J, Jennings PA, Adams JA. (2001). Structural characterization of protein kinase a as a function of nucleotide binding. hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection. J Biol Chem. 276(17), 14204-11. Wan KX, Gross J, Hillenkamp F, Gross ML. (2001). Fragmentation mechanisms of oligodeoxynucleotides studied by H/D exchange and electrospray ionization tandem mass spectrometry. J Am Soc Mass Spectrom. 12(2), 193-205. Mandell JG, Baerga-Ortiz A, Akashi S, Takio K, Komives EA. (2001). Solvent accessibility of the thrombin-thrombomodulin interface. J Mol Biol. 306(3), 575-89. Tuma R, Coward LU, Kirk MC, Barnes S, Prevelige PE Jr. (2001). Hydrogen-deuterium exchange as a probe of folding and assembly in viral capsids. J Mol Biol. 306(3), 389-96. Perez JM, Renisio JG, Prompers JJ, van Platerink CJ, Cambillau C, Darbon H,Frenken LG. (2001). Thermal unfolding of a llama antibody fragment: a two-state reversible process. Biochemistry. 40(1), 74-83.
2000 Demmers, J.A.A., Haverkamp, J., Heck, A.J.R., Koeppe II, R.E., and Killian, J.A.(2000) Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers. Proc. Natl. Acad. Sci. USA 97 3189-3194.
Raza A.S., Dharmasiri K., and Smith D.L., (2000). Identification of non-covalent structure in apocytochrome c by hydrogen exchange and mass spectrometry. J. Mass Spectrom. 35(5), 612-7. Eyles, S.J., Speir, P., Kruppa, G., Gierasch, L.M. & Kaltashov, I.A. (2000). Protein conformational stability probed by Fourier transform ion cyclotron resonance mass spectrometry. J. Am. Chem. Soc.122, 495-500 Chen J. and Smith D.L. (2000). Unfolding and disassembly of the chaperonin GroEL occurs via a tetradecameric intermediate with a folded equatorial domain. Biochemistry 39, 4250-4258. Tobler SA, Sherman NE, Fernandez EJ. (2000). Tracking lysozyme unfolding during salt-induced precipitation with hydrogen exchange and mass spectrometry. Biotechnol Bioeng.71(3), 194-207. Akashi S, Takio K. (2000). Characterization of the interface structure of enzyme-inhibitor complex by using hydrogen-deuterium exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Protein Sci. 9(12), 2497-505. Kheterpal I, Zhou S, Cook KD, Wetzel R. (2000). Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Proc Natl Acad Sci U S A. 97(25), 13597-601. Babu KR, Douglas DJ. (2000). Methanol-induced conformations of myoglobin at pH 4.0. Biochemistry 39(47), 14702-10. Pinheiro TJ, Cheng H, Seeholzer SH, Roder H. (2000). Direct evidence for the cooperative unfolding of cytochrome c in lipid membranes from H-(2)H exchange kinetics. J Mol Biol. 303(4), 617-26. Tito P, Nettleton EJ, Robinson CV. (2000). Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry. J Mol Biol. 303(2), 267-78. Buijs J, Hakansson K, Hagman C, Hakansson P, Oscarsson S. (2000). A new method for the accurate determination of the isotopic state of single amide hydrogens within peptides using Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun Mass Spectrom. 14(19), 1751-6. Ghaemmaghami S, Fitzgerald MC, Oas TG. (2000). A quantitative, high-throughput screen for protein stability. Proc Natl Acad Sci U S A. 97(15), 8296-301. Kraus M, Janek K, Bienert M, Krause E. (2000). Characterization of intermolecular beta-sheet peptides by mass spectrometry and hydrogen isotope exchange. Rapid Commun Mass Spectrom. 14(13), 1094-104. Arrington CB, Robertson AD. (2000).Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain. J Mol Biol. 300(1), 221-32. Palmer ME, Tetler LW, Wilson ID. (2000). Hydrogen/deuterium exchange using a coaxial sheath-flow interface for capillary electrophoresis/mass spectrometry. Rapid Commun Mass Spectrom. 14(9), 808-17. Villanueva J, Canals F, Villegas V, Querol E, Aviles FX. (2000). Hydrogen exchange monitored by MALDI-TOF mass spectrometry for rapid characterization of the stability and conformation of proteins. FEBS Lett. 472(1), 27-33. Faull KF, Higginson J, Waring AJ, To T, Whitelegge JP, Stevens RL, Fluharty CB, Fluharty AL. (2000). Hydrogen-deuterium exchange signature of porcine cerebroside sulfate activator protein. J Mass Spectrom. 35(3), 392-401. Jager M, Pluckthun A. (2000). Direct evidence by H/D exchange and ESI-MS for transient unproductive domain interaction in the refolding of an antibody scFv fragment. Protein Sci. 9(3), 552-63. Bouchard M, Benjamin DR, Tito P, Robinson CV, Dobson CM. (2000). Solvent effects on the conformation of the transmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry. Biophys J. 78(2), 1010-7. Hofstadler SA, Sannes-Lowery KA, Griffey RH. (2000). Enhanced gas-phase hydrogen-deuterium exchange of oligonucleotide and protein ions stored in an external multipole ion reservoir. J Mass Spectrom. 35(1), 62-70.
1999 Eyles, S.J., Dresch, T., Gierasch, L.M. & Kaltashov, I.A.. (1999). Unfolding dynamics of a beta-sheet protein studied by mass spectrometry. J. Mass Spectrom. 34, 1289-1295. Akashi S, Naito Y, Takio K. (1999). Observation of hydrogen-deuterium exchange of ubiquitin by direct analysis of electrospray capillary-skimmer dissociation with Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem. 71, 4974-4980. Nettleton EJ, Robinson CV.(1999). Probing conformations of amyloidogenic proteins by hydrogen exchange and mass spectrometry. Methods Enzymol.. 309, 633-646. Buijs J, Costa Vera C, Ayala E, Steensma E, Hakansson P, Oscarsson S. (1999). Conformational stability of adsorbed insulin studied with mass spectrometry and hydrogen exchange. Anal Chem. 71, 3219-3225. Deng, Y. and Smith, D.L.(1999). Hydrogen exchange demonstrates three domains in aldolase unfold sequentially. J. Mol. Biol. 294, 247-58. Deng, Y. and Smith, D.L. (1999). Rate and equilibrium constants for protein unfolding and refolding determined by hydrogen exchange-mass spectrometry. Anal. Biochem. 276, 150-60. Figueroa ID, Russell DH. (1999). Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes. J Am Soc Mass Spectrom. 10, 719-31. Nemirovskiy O, Giblin DE, Gross ML. (1999). Electrospray ionization mass spectrometry and hydrogen/deuterium exchange for probing the interaction of calmodulin with calcium. J Am Soc Mass Spectrom. 10, 711-718. Deng, Y, Zhang, Z. and Smith, D.L. (1999). Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics. J. Am. Soc. Mass Spectrom. 10, 675-684. Deng, Y. Pan, H. and Smith, D.L. (1999). Smith Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision induced dissociation mass spectrometry. J. Am. Chem. Soc. 121, 1966-1967. Engen, J.R., Gmeiner, W.H., Smithgall, T.E. and Smith, D.L. (1999). Comparison of SH3 and SH2 domain dynamics when expressed alone or in an SH(3+2) construct: The role of protein dynamics in functional regulation. J. Mol.Biol. 287, 645-656. Engen, J.R., Gmeiner, W.H., Smithgall, T.E. and Smith, D.L. (1999). Hydrogen exchange shows peptide binding stabilizes motions in Hck SH2. Biochemistry 38, 8926-8935. Deng, Y. and Smith, D.L. (1999). Identification of unfolding domains in large proteins by their unfolding rates. Biochemistry 37, 6256-6262.
1998 Wang, F., Scapin, G., Blanchard, J.S., and Angeletti, R.H. (1998). Substrate binding and conformational changes of Clostridium glutamicum diaminopimelate dehydrogenase revealed by hydrogen/deuterium, exchange and electrospray mass spectrometry. Protein Sci. 7, 293-299. Resing, K.A., and Ahn, N.G. (1998). Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1. Biochemistry 37, 463-475.
1997 Engen, J.R., Smithgall, T.E., Gmeiner, W.H., and Smith, D.L. (1997). Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry. Biochemistry 36, 14384-14391. Ramanathan, R., Gross, M.L., Zielinski, W.L., and Layloff, T.P. (1997). Monitoring recombinant protein drugs: a study of insulin by H/D exchange and electrospray ionization mass spectrometry. Anal. Chem. 69, 5142-5145. Dharmasiri, K., and Smith, D.L. (1997). Regional stability changes in oxidized and reduced cytochrome c located by hydrogen exchange and mass spectrometry. J. Am. Soc. Mass. Spectrom. 8, 1039-1045. Remigy, H., Jaquinod, M., Petillot, Y., Gagnon, J., Cheng, H., Xia, B., Markley, J.L., Hurley, J.K., Tollin, G., and Forest, E. (1997). Probing the influence of mutation on the stability of a ferredoxin by mass spectrometry. J. Protein Chem. 16, 527-532. Wang, F., Blanchard, J.S., and Tang, X.J. (1997). Hydrogen exchange/electrospray ionization mass spectrometry studies of substrate and inhibitor binding and conformational changes of Escherichia coli dihydrodipicolinate reductase. Biochemistry 36, 3755-3759. Yang, H., and Smith, D.L. (1997). Kinetics of cytochrome c folding examined by hydrogen exchange and mass spectrometry. Biochemistry 36, 14992-14999. Maier, C.S., Kim, O.H., and Deinzer, M.L. (1997). Conformational properties of the A-state of cytochrome s studied by hydrogen/deuterium exchange and electrospray mass spectrometry. Anal. Biochem. 252, 127-135. Zhang, Z., Li, W., Logan, T.M., Li, M., and Marshall, A.G. (1997). Human recombinant [C22A] FK506-binding protein amide hydrogen exchange rates from mass spectrometry match and extend those from NMR. Protein Sci. 6, 2203-2217.
1996 Wang, F., and Tang, X.-J. (1996). Conformational heterogeneity and stability of apomyoglobin studied by hydrogen-deuterium exchange and electrospray ionization mass spectrometry. Biochemistry 35, 4069-4078. Gross, M., Robinson, C.V., Mayhew, H., Hartl, F.U., and Radford, S.E. (1996). Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Sci. 5, 2506-2513. Jaquinod, M., Guy, P., Halgand, F., Caffrey, M., Fitch, J., Cusanovich, M., and Forest, E. (1996). Stability of Rhodobacter capsulatus ferrocytochrome c2 wild-type and site-directed mutants using hydrogen/deuterium exchange monitored by electrospray ionization mass spectrometry. FEBS Lett. 380, 44-48. Guy, P., Remigy, H., Jaquinod, M., Bersch, B., Blanchard, L., Dolla, A., and Forest, E. (1996). Study of the new stability properties induced by amino acid replacement of tyrosine 64 in cytochrome C553 from Desulfobibrio vulgaris Hildenborough using electrospray ionization mass spectrometry. Biochem. Biophys. Res. Commun. 218, 97-103. Guy, P., Jaquinod, M., Remigy, H., Andrieu, J.P., Gagnon, J., Bersch, B., Dolla, A., Blanchard, L., Guerlesquin, F., and Forest, E. (1996). New conformational properties induced by the replacement of Tyr-64 in Desulfovibrio vulgaris Hildenborough ferricytochrome d553 using isotopic exchange monitored by mass spectrometry. FEBS Lett. 395, 53-57. Dharmasiri, K., and Smith, D.L. (1996). Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins. Anal. Chem. 68, 2340-2344. Zhang, Z., Post, C.B., and Smith, D.L. (1996). Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase. Biochemistry 35, 779-791. Zhang, Z., and Smith, D.L. (1996). Thermal-induced unfolding domains in aldolase by amide hydrogen exchange and mass spectrometry. Protein Sci. 5, 1282-1289.
1995 Kragelund, B.B., Knudsen, J., and Poulsen, F.M. (1995). Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP). J. Mol. Biol 250, 695-706. Anderegg, R.J., and Wagner, D.S. (1995). Mass spectrometric characterization of a protein ligand interaction. J. Am. Chem. Soc. 117, 1374-1377.
1994 Robinson, C.V., Gross, M., Eyles, S.J., Ewbank, J.J., Mayhew, M., Hartl, F.U., Dobson, C.M., and Radford, S.E. (1994). Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry. Nature 372, 646-651. Ohguro, H., Palczewski, K., Walsh, K.A., and Johnson, R.S. (1994). Topographic study of arrestin using differential chemical modifications and hydrogen/deuterium exchange. Protein Sci. 3, 2428-2434. Johnson, R.S., and Walsh, K.A. (1994). Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin. Protein Sci. 3, 2411-2418. Liu, Y., and Smith, D.L. (1994). Probing high order structure of proteins by fast-atom bombardment mass spectrometry. J. Am. Soc. Mass Spectrom. 5, 19-28.
1993 Zhang, Z., and Smith, D.L. (1993). Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation. Protein Sci. 2, 522-531. Miranker, A., Robinson, C.V., Radford, S.E., Aplin, R.T., and Dobson, C.M. (1993). Detection of transient protein folding populations by mass spectrometry. Science 262, 896-900.
1992 G. Thèvenon, J. Kozlowski, Z. Zhang, and D.L. Smith (1992). Determination of Amide Hydrogen Exchange Rates in Peptides by Mass Spectrometry. Anal. Chem. 64, 2456-2458.
1991 Katta, V., and Chait, B.T. (1991). Conformational changes in proteins probed by hydrogen- exchange electrospray-ionization mass spectrometry. Rapid Commun. Mass Spectrom. 5, 214-217.
pre 1990 Miyano, H., Suzuki, E., Akashi, S., Furuya, M., Tsuji, T., Hirayama, K. and Nagashima, N. (1989). Histidine Microenvironment Analyses of Recombinant Human Interleukin-2 by Fast Atom Bombardment Mass Spectrometry and Proton Magnetic Resonance Spectrometry. Anal. Sci. 5, 759-761. Rosa, J.J., and Richards, F.M. (1979). An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: application to ribonuclease S peptide. J. Mol. Biol. 133, 399-416. Rosa, J.J., and Richards, F.M. (1981). Hydrogen exchange from identified regions of the S-protein component of ribonuclease as a function of temperature, pH, and the binding of S-peptide. J. Mol. Biol. 145, 835-851. Englander, J.J., Rogero, J.R., and Englander, S.W. (1985). Protein hydrogen exchange studied by the fragment separation method. Anal. Biochem. 147, 234-244.
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