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Study of a noncovalent trp repressor:DNA operator complex by electrospray time-of-flight mass spectrometry
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The role of the 6 lysines and the terminal amine of Escherichia coli single-strand binding protein in its binding of single-stranded DNA
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Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry
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Rapid analysis of epitope-paratope interactions between HIV-1 and a 17-amino-acid neutralizing microantibody by electrospray ionization mass spectrometry
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A peptide derived from the gp120 envelope glycoprotein of HIV-1 is seen to interact with a specific antibody. Key residues for the interaction are determined, by digestion of the peptide
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Counting individual sulfur atoms in a protein by ultra-high resolution Fourier transform ion cyclotron resonance mass spectrometry: Experimental resolution of isotropic fine structure in proteins
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Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
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Changes in the dynamics of the enzyme are revealed by comparing hydrogen exchange mass spectrometry (MS) data of the free and ligand-bound species. Previous crystal structures comparing ligand-free and ligand-bound proteins reveal a flexible loop that closes around an inhibitor. MS reveals that residues screened by closure of this loop have increased protection from HX, and also that regions of the protein that are very similar in the crystal structures have altered HX protection
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Wang F, Li WQ, Emmett MR, Hendrickson CL, Marshall AG, Zhang YL, Wu L, Zhang ZY Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Biochemistry. 37:1998;15289-15299. Changes in the dynamics of the enzyme are revealed by comparing hydrogen exchange mass spectrometry (MS) data of the free and ligand-bound species. Previous crystal structures comparing ligand-free and ligand-bound proteins reveal a flexible loop that closes around an inhibitor. MS reveals that residues screened by closure of this loop have increased protection from HX, and also that regions of the protein that are very similar in the crystal structures have altered HX protection.
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0033515632
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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
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Interdomain interactions are shown to alter the dynamics of the individual domains, reflected in alteration of HX characteristics
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Defining protein ensembles with native state NH exchange: Kinetics of interconversion and cooperative units from combined NMR and MS analysis
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NMR-derived HX data of the turkey ovomucoid domain are used to simulate peak widths during mass spectrometry (MS) exchange. Observed MS peaks do not match these, suggesting that the extent of cooperativity is more limited than suggested using NMR
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0033620364
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Electron capture dissociation of gaseous multiply charged proteins is favoured at disulphide bonds and other sites of high hydrogen atom affinity
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The electron capture dissociation method was shown to generate preferential cleavage of the backbone at disulfide bonds, in contrast to excitation of the ions by photons or low-energy collisions
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Zubarev RA, Kruger NA, Frediksson EK, Lewis MA, Horn DM, Carpenter BK, McLafferty FW Electron capture dissociation of gaseous multiply charged proteins is favoured at disulphide bonds and other sites of high hydrogen atom affinity. J Am Chem Soc. 121:1999;2857-2862. The electron capture dissociation method was shown to generate preferential cleavage of the backbone at disulfide bonds, in contrast to excitation of the ions by photons or low-energy collisions.
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0033541119
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Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry
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Hydrogen/deuterium exchange experiments can give site-specific information on the exposure to or protection from solvent of all residues only if the deuterium label remains fixed during digestion, ionisation and fragmentation of proteins. Using cytochrome c as a model, the authors present evidence that the label is not scrambled during peptic digestion or collision-induced dissociation if the b-ions are monitored, as the mass spectrometry results closely match those observed by NMR methods
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Deng YZ, Pan H, Smith DL 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. 121:1999;1966-1967. Hydrogen/deuterium exchange experiments can give site-specific information on the exposure to or protection from solvent of all residues only if the deuterium label remains fixed during digestion, ionisation and fragmentation of proteins. Using cytochrome c as a model, the authors present evidence that the label is not scrambled during peptic digestion or collision-induced dissociation if the b-ions are monitored, as the mass spectrometry results closely match those observed by NMR methods.
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A near-native state on the slow refolding pathway of hen lysozyme
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GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism
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Coyle JE, Texter FL, Ashcroft AE, Masselos D, Robinson CV, Radford SE GroEL accelerates the refolding of hen lysozyme without changing its folding mechanism. Nat Struct Biol. 6:1999;683-690.
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Characterisation of the dominant oxidative folding intermediate of hen lysozyme
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in press. The refolding of hen egg white lysozyme from a fully unfolded species with reduced cysteine residues is shown to proceed via a stable intermediate with three correctly formed disulfide bonds. The unformed bond is identified by accurate mass measurement by Fourier-transform mass spectrometry (FTMS) followed by digestion of the intermediate and tandem MS of the fragments
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van den Berg B, Chung EW, Robinson CV, Dobson CM Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999;. in press. The refolding of hen egg white lysozyme from a fully unfolded species with reduced cysteine residues is shown to proceed via a stable intermediate with three correctly formed disulfide bonds. The unformed bond is identified by accurate mass measurement by Fourier-transform mass spectrometry (FTMS) followed by digestion of the intermediate and tandem MS of the fragments.
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J Mol Biol
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Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate
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Tsui V, Garcia C, Cavagnero S, Siuzdak G, Dyson HJ, Wright PE Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate. Protein Sci. 8:1999;45-49.
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Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin
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Booth DR, Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CCF, Pepys MB Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature. 385:1997;787-793.
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Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behaviour in its disease related variants
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Human lysozyme variants are shown to refold via short-lived intermediates. One of the variants has markedly different refolding kinetics, observed by the increased lifetime of an intermediate state
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Canet D, Sunde M, Last AM, Miranker A, Spencer A, Robinson CV, Dobson CM Mechanistic studies of the folding of human lysozyme and the origin of amyloidogenic behaviour in its disease related variants. Biochemistry. 38:1999;6419-6427. Human lysozyme variants are shown to refold via short-lived intermediates. One of the variants has markedly different refolding kinetics, observed by the increased lifetime of an intermediate state.
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(1999)
Biochemistry
, vol.38
, pp. 6419-6427
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Canet, D.1
Sunde, M.2
Last, A.M.3
Miranker, A.4
Spencer, A.5
Robinson, C.V.6
Dobson, C.M.7
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38
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0032555738
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Protein subunit interactions and structural integrity of amyloidogenic transthyretins: Evidence from electrospray mass spectrometry
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The effect of amyloidogenic mutations on the stability of the transthyretin tetramer is shown by comparing the ease of dissociation of the variants with the wild type
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Nettleton EJ, Sunde M, Lai ZH, Kelly JW, Dobson CM, Robinson CV Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J, Mol, Biol. 281:1998;553-564. The effect of amyloidogenic mutations on the stability of the transthyretin tetramer is shown by comparing the ease of dissociation of the variants with the wild type.
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(1998)
J, Mol, Biol
, vol.281
, pp. 553-564
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Nettleton, E.J.1
Sunde, M.2
Lai, Z.H.3
Kelly, J.W.4
Dobson, C.M.5
Robinson, C.V.6
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39
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0032125821
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Detection of a monomeric intermediate associated with dimerization of protein HU by mass spectrometry
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The stability of the DNA-binding protein HU is shown to increase with salt concentration. Mass spectrometry also reveals an intermediate, partially folded monomer, which is formed at low salt concentration
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Vis H, Heinemann U, Dobson CM, Robinson CV Detection of a monomeric intermediate associated with dimerization of protein HU by mass spectrometry. J Am Chem Soc. 120:1998;6427-6428. The stability of the DNA-binding protein HU is shown to increase with salt concentration. Mass spectrometry also reveals an intermediate, partially folded monomer, which is formed at low salt concentration.
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(1998)
J Am Chem Soc
, vol.120
, pp. 6427-6428
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Vis, H.1
Heinemann, U.2
Dobson, C.M.3
Robinson, C.V.4
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40
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0344655671
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Selective association of protein molecules followed by mass spectrometry
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Vis H, Dobson CM, Robinson CV Selective association of protein molecules followed by mass spectrometry. Protein Sci. 8:1999;1368-1370.
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(1999)
Protein Sci
, vol.8
, pp. 1368-1370
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Vis, H.1
Dobson, C.M.2
Robinson, C.V.3
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41
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0032939173
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Crystallographically identical virus capsids display different properties in solution
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The dynamics of crystallographically identical virus structures are markedly different, despite their identical crystal structures. The recombinant virus, containing a random segment of RNA, is both more rapidly digested and more susceptible to covalent modification than the wild type, which contains the correct viral RNA
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Bothner B, Schneemann A, Marshall D, Reddy V, Johnson JE, Siuzdak G Crystallographically identical virus capsids display different properties in solution. Nat Struct Biol. 6:1999;114-116. The dynamics of crystallographically identical virus structures are markedly different, despite their identical crystal structures. The recombinant virus, containing a random segment of RNA, is both more rapidly digested and more susceptible to covalent modification than the wild type, which contains the correct viral RNA.
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(1999)
Nat Struct Biol
, vol.6
, pp. 114-116
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Bothner, B.1
Schneemann, A.2
Marshall, D.3
Reddy, V.4
Johnson, J.E.5
Siuzdak, G.6
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42
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0032499729
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Antiviral agent blocks breathing of the common cold virus
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X-ray analysis shows that the envelope protein VP4 appears to be buried near the core of human rhinovirus 14, yet is amenable to digestion by trypsin. This shows the large dynamic motions that occur even in this relatively large structure
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Lewis JK, Bothner B, Smith TJ, Siuzdak G Antiviral agent blocks breathing of the common cold virus. Proc Natl Acad Sci USA. 95:1998;6774-6778. X-ray analysis shows that the envelope protein VP4 appears to be buried near the core of human rhinovirus 14, yet is amenable to digestion by trypsin. This shows the large dynamic motions that occur even in this relatively large structure.
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(1998)
Proc Natl Acad Sci USA
, vol.95
, pp. 6774-6778
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Lewis, J.K.1
Bothner, B.2
Smith, T.J.3
Siuzdak, G.4
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43
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0032247077
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Dissection of multi-protein complexes using mass spectrometry - subunit interactions in transthyretin and retinol-binding protein complexes
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Rostom AA, Sunde M, Richardson SJ, Schreiber G, Jarvis S, Bateman R, Dobson CM, Robinson CV Dissection of multi-protein complexes using mass spectrometry - subunit interactions in transthyretin and retinol-binding protein complexes. Proteins. 2(suppl):1998;3-11.
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(1998)
Proteins
, vol.2
, Issue.SUPPL.
, pp. 3-11
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Rostom, A.A.1
Sunde, M.2
Richardson, S.J.3
Schreiber, G.4
Jarvis, S.5
Bateman, R.6
Dobson, C.M.7
Robinson, C.V.8
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44
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0032560474
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Mass spectrometry of ribosomes and ribosomal subunits
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Despite its impressive size, the ribosome can be studied by mass spectrometry. Dissociation products reveal which of the subunits interact strongly, and HX shows how flexible these subunits are within the intact complex
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Benjamin DR, Robinson CV, Hendrick JP, Hartl FU, Dobson CM Mass spectrometry of ribosomes and ribosomal subunits. Proc Natl Acad Sci USA. 93:1998;7391-7395. Despite its impressive size, the ribosome can be studied by mass spectrometry. Dissociation products reveal which of the subunits interact strongly, and HX shows how flexible these subunits are within the intact complex.
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(1998)
Proc Natl Acad Sci USA
, vol.93
, pp. 7391-7395
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Benjamin, D.R.1
Robinson, C.V.2
Hendrick, J.P.3
Hartl, F.U.4
Dobson, C.M.5
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45
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0033583731
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Detection of the intact GroEL chaperonin assembly by mass spectrometry
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The large macromolecular complex of GroEL can be maintained intact in the gas phase. Known connectivities are seen to be preserved upon collision-induced dissociation of the complex, showing that this method could be used to study species where the links are unknown
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Rostom AA, Robinson CV Detection of the intact GroEL chaperonin assembly by mass spectrometry. J Am Chem Soc. 121:1999;4718-4719. The large macromolecular complex of GroEL can be maintained intact in the gas phase. Known connectivities are seen to be preserved upon collision-induced dissociation of the complex, showing that this method could be used to study species where the links are unknown.
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(1999)
J Am Chem Soc
, vol.121
, pp. 4718-4719
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Rostom, A.A.1
Robinson, C.V.2
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46
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0032872914
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Disassembly of intact multiprotein complexes in the gas phase
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Rostom AA, Robinson CV Disassembly of intact multiprotein complexes in the gas phase. Curr Opin Struct Biol. 9:1999;135-141.
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(1999)
Curr Opin Struct Biol
, vol.9
, pp. 135-141
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Rostom, A.A.1
Robinson, C.V.2
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