Protein Microarrays for High Throughput Hydrogen/Deuterium Exchange Monitored by FTIR Imaging
Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) h...
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| Published in: | International journal of molecular sciences Vol. 25; no. 18; p. 9989 |
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| Abstract | Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) has long been used to evaluate protein structure and dynamics. The rate of exchange constitutes a sensitive marker of the conformational state of the protein and of its stability. It is often monitored by mass spectrometry. Fourier transform infrared (FTIR) spectroscopy is another method with very promising capabilities. Combining protein microarrays with FTIR imaging resulted in high throughput HDX FTIR measurements. BaF2 slides bearing the protein microarrays were covered by another slide separated by a spacer, allowing us to flush the cell continuously with a flow of N2 gas saturated with 2H2O. Exchange occurred simultaneously for all proteins and single images covering ca. 96 spots of proteins that could be recorded on-line at selected time points. Each protein spot contained ca. 5 ng protein, and the entire array covered 2.5 × 2.5 mm2. Furthermore, HDX could be monitored in real time, and the experiment was therefore not subject to back-exchange problems. Analysis of HDX curves by inverse Laplace transform and by fitting exponential curves indicated that quantitative comparison of the samples is feasible. The paper also demonstrates how the whole process of analysis can be automatized to yield fast analyses. |
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| AbstractList | Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) has long been used to evaluate protein structure and dynamics. The rate of exchange constitutes a sensitive marker of the conformational state of the protein and of its stability. It is often monitored by mass spectrometry. Fourier transform infrared (FTIR) spectroscopy is another method with very promising capabilities. Combining protein microarrays with FTIR imaging resulted in high throughput HDX FTIR measurements. BaF2 slides bearing the protein microarrays were covered by another slide separated by a spacer, allowing us to flush the cell continuously with a flow of N2 gas saturated with 2H2O. Exchange occurred simultaneously for all proteins and single images covering ca. 96 spots of proteins that could be recorded on-line at selected time points. Each protein spot contained ca. 5 ng protein, and the entire array covered 2.5 × 2.5 mm2. Furthermore, HDX could be monitored in real time, and the experiment was therefore not subject to back-exchange problems. Analysis of HDX curves by inverse Laplace transform and by fitting exponential curves indicated that quantitative comparison of the samples is feasible. The paper also demonstrates how the whole process of analysis can be automatized to yield fast analyses. Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) has long been used to evaluate protein structure and dynamics. The rate of exchange constitutes a sensitive marker of the conformational state of the protein and of its stability. It is often monitored by mass spectrometry. Fourier transform infrared (FTIR) spectroscopy is another method with very promising capabilities. Combining protein microarrays with FTIR imaging resulted in high throughput HDX FTIR measurements. BaF[sub.2] slides bearing the protein microarrays were covered by another slide separated by a spacer, allowing us to flush the cell continuously with a flow of N[sub.2] gas saturated with [sup.2] H[sub.2] O. Exchange occurred simultaneously for all proteins and single images covering ca. 96 spots of proteins that could be recorded on-line at selected time points. Each protein spot contained ca. 5 ng protein, and the entire array covered 2.5 × 2.5 mm[sup.2] . Furthermore, HDX could be monitored in real time, and the experiment was therefore not subject to back-exchange problems. Analysis of HDX curves by inverse Laplace transform and by fitting exponential curves indicated that quantitative comparison of the samples is feasible. The paper also demonstrates how the whole process of analysis can be automatized to yield fast analyses. Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) has long been used to evaluate protein structure and dynamics. The rate of exchange constitutes a sensitive marker of the conformational state of the protein and of its stability. It is often monitored by mass spectrometry. Fourier transform infrared (FTIR) spectroscopy is another method with very promising capabilities. Combining protein microarrays with FTIR imaging resulted in high throughput HDX FTIR measurements. BaF slides bearing the protein microarrays were covered by another slide separated by a spacer, allowing us to flush the cell continuously with a flow of N gas saturated with H O. Exchange occurred simultaneously for all proteins and single images covering ca. 96 spots of proteins that could be recorded on-line at selected time points. Each protein spot contained ca. 5 ng protein, and the entire array covered 2.5 × 2.5 mm . Furthermore, HDX could be monitored in real time, and the experiment was therefore not subject to back-exchange problems. Analysis of HDX curves by inverse Laplace transform and by fitting exponential curves indicated that quantitative comparison of the samples is feasible. The paper also demonstrates how the whole process of analysis can be automatized to yield fast analyses. Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) has long been used to evaluate protein structure and dynamics. The rate of exchange constitutes a sensitive marker of the conformational state of the protein and of its stability. It is often monitored by mass spectrometry. Fourier transform infrared (FTIR) spectroscopy is another method with very promising capabilities. Combining protein microarrays with FTIR imaging resulted in high throughput HDX FTIR measurements. BaF2 slides bearing the protein microarrays were covered by another slide separated by a spacer, allowing us to flush the cell continuously with a flow of N2 gas saturated with 2H2O. Exchange occurred simultaneously for all proteins and single images covering ca. 96 spots of proteins that could be recorded on-line at selected time points. Each protein spot contained ca. 5 ng protein, and the entire array covered 2.5 × 2.5 mm2. Furthermore, HDX could be monitored in real time, and the experiment was therefore not subject to back-exchange problems. Analysis of HDX curves by inverse Laplace transform and by fitting exponential curves indicated that quantitative comparison of the samples is feasible. The paper also demonstrates how the whole process of analysis can be automatized to yield fast analyses.Proteins form the fastest-growing therapeutic class. Due to their intrinsic instability, loss of native structure is common. Structure alteration must be carefully evaluated as structural changes may jeopardize the efficiency and safety of the protein-based drugs. Hydrogen deuterium exchange (HDX) has long been used to evaluate protein structure and dynamics. The rate of exchange constitutes a sensitive marker of the conformational state of the protein and of its stability. It is often monitored by mass spectrometry. Fourier transform infrared (FTIR) spectroscopy is another method with very promising capabilities. Combining protein microarrays with FTIR imaging resulted in high throughput HDX FTIR measurements. BaF2 slides bearing the protein microarrays were covered by another slide separated by a spacer, allowing us to flush the cell continuously with a flow of N2 gas saturated with 2H2O. Exchange occurred simultaneously for all proteins and single images covering ca. 96 spots of proteins that could be recorded on-line at selected time points. Each protein spot contained ca. 5 ng protein, and the entire array covered 2.5 × 2.5 mm2. Furthermore, HDX could be monitored in real time, and the experiment was therefore not subject to back-exchange problems. Analysis of HDX curves by inverse Laplace transform and by fitting exponential curves indicated that quantitative comparison of the samples is feasible. The paper also demonstrates how the whole process of analysis can be automatized to yield fast analyses. |
| Audience | Academic |
| Author | De Meutter, Joëlle Goormaghtigh, Erik |
| AuthorAffiliation | Center for Structural Biology and Bioinformatics, Laboratory for the Structure and Function of Biological Membranes, Campus Plaine, Université Libre de Bruxelles CP206/2, B1050 Brussels, Belgium |
| AuthorAffiliation_xml | – name: Center for Structural Biology and Bioinformatics, Laboratory for the Structure and Function of Biological Membranes, Campus Plaine, Université Libre de Bruxelles CP206/2, B1050 Brussels, Belgium |
| Author_xml | – sequence: 1 givenname: Joëlle surname: De Meutter fullname: De Meutter, Joëlle – sequence: 2 givenname: Erik orcidid: 0000-0002-2071-2262 surname: Goormaghtigh fullname: Goormaghtigh, Erik |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39337477$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1038/284572a0 10.1177/00037028241231824 10.1016/j.saa.2008.08.008 10.1366/0003702963904610 10.1021/acs.biochem.6b00403 10.1016/S0021-9673(02)01357-2 10.1002/bip.21022 10.1021/jasms.3c00285 10.1002/pro.2081 10.1002/bip.1980.360190509 10.1021/ac502529q 10.1002/bip.1975.360140402 10.1021/acs.analchem.0c03943 10.1016/j.drudis.2013.07.019 10.1366/000370204322729496 10.1371/journal.pone.0082118 10.1016/j.bpj.2009.08.045 10.1017/S0033583597003375 10.1007/s00249-021-01502-y 10.1016/j.saa.2020.118636 10.1016/0079-6107(93)90006-6 10.1016/j.bbalip.2013.10.010 10.1002/pro.5074 10.1021/acs.analchem.0c03677 10.1016/0167-4838(89)90075-7 10.1021/bi971337p 10.3233/BSI-160137 10.1074/jbc.271.38.23089 10.1016/j.jasms.2008.11.010 10.1016/0167-4838(86)90024-5 10.1042/BJ20040277 10.1007/s11095-020-02897-7 10.1074/jbc.271.40.24617 10.1021/bi00105a033 10.1016/0165-022X(79)90021-6 10.1021/bi0204950 10.1017/S0033583500005217 10.1039/C6AN02048H 10.1002/j.1460-2075.1985.tb03821.x 10.1006/abio.1997.2502 10.1038/335694a0 10.1002/9780470027318.a9792 10.1073/pnas.1411798111 10.1021/bi010017+ 10.1016/S0021-9258(18)47000-7 10.1073/pnas.1232301100 10.1016/S0021-9258(17)35695-8 10.1016/j.tibtech.2014.05.005 10.1016/0010-4655(82)90174-6 10.1016/j.aca.2020.03.038 10.1366/000370205774783115 10.1016/j.ab.2004.10.016 10.1073/pnas.95.17.9903 10.1529/biophysj.107.125856 10.1007/978-1-4939-7151-0_13 10.1021/bi00323a018 10.1002/bip.20035 10.1111/j.1432-1033.1995.659_2.x 10.1016/j.xphs.2016.07.006 10.1002/bip.360240203 10.1021/acs.analchem.0c02663 10.1021/bi00390a040 10.1074/jbc.272.1.262 10.1021/bi00491a012 10.1021/ja984208k 10.1021/acs.analchem.9b05724 10.1002/pro.2082 10.1002/pro.5560020404 10.1371/journal.pone.0176748 10.1016/j.bbabio.2007.06.004 10.1038/nrd3746 10.1016/j.trac.2017.12.002 10.1016/j.csbj.2020.07.001 |
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| Keywords | protein microarrays hydrogen deuterium exchange FTIR spectroscopy |
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| References | Derenne (ref_31) 2014; 1841 Dreissig (ref_32) 2009; 71 Iloro (ref_63) 2008; 94 Goormaghtigh (ref_50) 1996; 50 Zhang (ref_5) 2020; 92 Grimard (ref_22) 2001; 40 Tamm (ref_36) 1997; 30 Haris (ref_15) 1986; 874 Wilcox (ref_28) 2016; 55 Wei (ref_3) 2014; 19 Chirgadze (ref_47) 1975; 14 Haris (ref_53) 1995; 233 ref_17 Grdadolnik (ref_64) 2005; 59 Gregory (ref_73) 1985; 24 Provencher (ref_75) 1979; 1 Raussens (ref_43) 1996; 271 Roberts (ref_1) 2014; 32 Skinner (ref_60) 2012; 21 (ref_7) 2024; 35 Zhang (ref_8) 1993; 2 Vigano (ref_16) 2004; 74 Goormaghtigh (ref_44) 2021; 50 Englander (ref_58) 2014; 111 Goormaghtigh (ref_49) 2009; 2 Goormaghtigh (ref_40) 2020; 18 Jakubek (ref_14) 2018; 103 Haris (ref_52) 1989; 995 Fang (ref_68) 2020; 37 Careri (ref_67) 1980; 284 Barth (ref_45) 2007; 1767 Downer (ref_51) 1986; 261 Goormaghtigh (ref_56) 1997; 36 Kleffel (ref_54) 1985; 4 Lam (ref_10) 2002; 982 Scheirlinckx (ref_20) 2004; 382 Krimm (ref_37) 1986; 38 Pastrana (ref_55) 1991; 30 ref_35 ref_33 Skinner (ref_61) 2012; 21 Schinkel (ref_66) 1985; 24 Sonveaux (ref_21) 1996; 271 Derfoufi (ref_69) 2016; 5 Vandenameele (ref_70) 2017; 142 Knox (ref_72) 1980; 19 Neehaul (ref_62) 2017; 1635 ref_38 Tuchsen (ref_57) 1987; 26 Raussens (ref_48) 2004; 58 Meskers (ref_65) 1999; 121 Wang (ref_23) 2008; 89 Raussens (ref_19) 1997; 272 Lee (ref_26) 1990; 29 Byrne (ref_39) 2014; 86 Englander (ref_59) 1983; 16 Pastrana (ref_34) 2021; 93 Berkowitz (ref_4) 2012; 11 Zhang (ref_12) 2009; 20 Goormaghtigh (ref_71) 2021; 93 Nazari (ref_11) 2016; 105 Goormaghtigh (ref_29) 2021; 93 Arrondo (ref_25) 1993; 59 Englander (ref_9) 2003; 100 Navea (ref_24) 2005; 336 Derenne (ref_30) 2020; 1112 ref_2 Provencher (ref_74) 1982; 27 Goormaghtigh (ref_27) 2009; 97 Hilser (ref_6) 1998; 95 Hollecker (ref_42) 2002; 41 Ye (ref_41) 2024; 33 Goormaghtigh (ref_18) 1994; 269 Udgaonkar (ref_13) 1988; 335 Rahmelow (ref_46) 1998; 257 |
| References_xml | – volume: 284 start-page: 572 year: 1980 ident: ref_67 article-title: Correlation of IR Spectroscopic, Heat Capacity, Diamagnetic Susceptibility and Enzymatic Measurements on Lysozyme Powder publication-title: Nature doi: 10.1038/284572a0 – ident: ref_35 doi: 10.1177/00037028241231824 – volume: 71 start-page: 2069 year: 2009 ident: ref_32 article-title: Quantification of Brain Lipids by FTIR Spectroscopy and Partial Least Squares Regression publication-title: Spectrochim. Acta A doi: 10.1016/j.saa.2008.08.008 – volume: 50 start-page: 1519 year: 1996 ident: ref_50 article-title: Relevance of Protein Thin Films Prepared for Attenuated Total Reflection Fourier Transform Infrared Spectroscopy: Significance of the PH publication-title: Appl. Spectrosc. doi: 10.1366/0003702963904610 – volume: 55 start-page: 3794 year: 2016 ident: ref_28 article-title: Determination of Protein Secondary Structure from Infrared Spectra Using Partial Least-Squares Regression publication-title: Biochemistry doi: 10.1021/acs.biochem.6b00403 – volume: 982 start-page: 85 year: 2002 ident: ref_10 article-title: Mapping of Protein:Protein Contact Surfaces by Hydrogen/Deuterium Exchange, Followed by on-Line High-Performance Liquid Chromatography-Electrospray Ionization Fourier-Transform Ion-Cyclotron-Resonance Mass Analysis publication-title: J. Chromatogr. A doi: 10.1016/S0021-9673(02)01357-2 – volume: 89 start-page: 895 year: 2008 ident: ref_23 article-title: Determination of the Secondary Structure of Proteins in Different Environments by FTIR-ATR Spectroscopy and PLS Regression publication-title: Biopolymers doi: 10.1002/bip.21022 – volume: 38 start-page: 181 year: 1986 ident: ref_37 article-title: Vibrational Spectroscopy and Conformation of Peptides, Polypeptides and Proteins publication-title: Adv. Prot. Chem. – volume: 35 start-page: 197 year: 2024 ident: ref_7 article-title: Deep Learning Enables Automatic Correction of Experimental HDX-MS Data with Applications in Protein Modeling publication-title: J. Am. Soc. Mass Spectrom. doi: 10.1021/jasms.3c00285 – volume: 21 start-page: 996 year: 2012 ident: ref_61 article-title: Protein Dynamics Viewed by Hydrogen Exchange publication-title: Protein Sci. doi: 10.1002/pro.2081 – volume: 19 start-page: 1049 year: 1980 ident: ref_72 article-title: Fluctuations of Protein Structure as Expressed in the Distribution of Hydrogen Exchange Rate Constants publication-title: Biopolymers doi: 10.1002/bip.1980.360190509 – volume: 86 start-page: 9786 year: 2014 ident: ref_39 article-title: High-Throughput Thermal Stability Analysis of a Monoclonal Antibody by Attenuated Total Reflection FT-IR Spectroscopic Imaging publication-title: Anal. Chem. doi: 10.1021/ac502529q – volume: 14 start-page: 679 year: 1975 ident: ref_47 article-title: Estimation of Amino Acid Residue Side-Chain Absorption in the Infrared Spectra of Protein Solutions in Heavy Water publication-title: Biopolymers doi: 10.1002/bip.1975.360140402 – volume: 93 start-page: 1561 year: 2021 ident: ref_71 article-title: Searching for a Better Match between Protein Secondary Structure Definitions and Protein FTIR Spectra publication-title: Anal. Chem. doi: 10.1021/acs.analchem.0c03943 – volume: 19 start-page: 95 year: 2014 ident: ref_3 article-title: Hydrogen/Deuterium Exchange Mass Spectrometry for Probing Higher Order Structure of Protein Therapeutics: Methodology and Applications publication-title: Drug Discov. Today doi: 10.1016/j.drudis.2013.07.019 – volume: 58 start-page: 68 year: 2004 ident: ref_48 article-title: Analysis of H-1/H-2 Exchange Kinetics Using Model Infrared Spectra publication-title: Appl. Spectrosc. doi: 10.1366/000370204322729496 – ident: ref_17 doi: 10.1371/journal.pone.0082118 – volume: 97 start-page: 2736 year: 2009 ident: ref_27 article-title: Pulmonary Surfactant Protein SP-C Counteracts the Deleterious Effects of Cholesterol on the Activity of Surfactant Films under Physiologically Relevant Compression-Expansion Dynamics publication-title: Biophys. J. doi: 10.1016/j.bpj.2009.08.045 – volume: 30 start-page: 365 year: 1997 ident: ref_36 article-title: Infrared Spectroscopy of Proteins and Peptides in Lipid Bilayer publication-title: Q. Rev. Biophys. doi: 10.1017/S0033583597003375 – volume: 50 start-page: 613 year: 2021 ident: ref_44 article-title: Evaluation of Protein Secondary Structure from FTIR Spectra Improved after Partial Deuteration publication-title: Eur. Biophys. J. doi: 10.1007/s00249-021-01502-y – ident: ref_38 doi: 10.1016/j.saa.2020.118636 – volume: 59 start-page: 23 year: 1993 ident: ref_25 article-title: Quantitative Studies of the Structure of Proteins in Solution by Fourier-Transform Infrared Spectroscopy publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/0079-6107(93)90006-6 – volume: 1841 start-page: 1200 year: 2014 ident: ref_31 article-title: Lipid Quantification Method Using FTIR Spectroscopy Applied on Cancer Cell Extracts publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbalip.2013.10.010 – volume: 33 start-page: e5074 year: 2024 ident: ref_41 article-title: Probe Capsid Structure Stability and Dynamics of Adeno-Associated Virus as an Important Viral Vector for Gene Therapy by Hydrogen-Deuterium Exchange-Mass Spectrometry publication-title: Protein Sci. doi: 10.1002/pro.5074 – volume: 93 start-page: 3733 year: 2021 ident: ref_29 article-title: FTIR Imaging of Protein Microarrays for High Throughput Secondary Structure Determination publication-title: Anal. Chem. doi: 10.1021/acs.analchem.0c03677 – volume: 995 start-page: 160 year: 1989 ident: ref_52 article-title: Fourier Transform Infrared Spectroscopic Investigation of Rhodopsin Structure and Its Comparison with Bacteriorhodopsin publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(89)90075-7 – volume: 36 start-page: 13603 year: 1997 ident: ref_56 article-title: Amide-Proton Exchange of Water-Soluble Proteins of Different Structural Classes Studied at the Submolecular Level by Infrared Spectroscopy publication-title: Biochemistry doi: 10.1021/bi971337p – volume: 5 start-page: 145 year: 2016 ident: ref_69 article-title: Analysis of Protein Microarrays by FTIR Imaging publication-title: Biomed. Spectrosc. Imaging doi: 10.3233/BSI-160137 – volume: 271 start-page: 23089 year: 1996 ident: ref_43 article-title: Hydrogen/Deuterium Exchange Kinetics of Apolipophorin-III in Lipid-Free and Phospholipid-Bound States. An Analysis by Fourier Transform Infrared Spectroscopy publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.38.23089 – volume: 20 start-page: 520 year: 2009 ident: ref_12 article-title: Fast Reversed-Phase Liquid Chromatography to Reduce Back Exchange and Increase Throughput in H/D Exchange Monitored by FT-ICR Mass Spectrometry publication-title: J. Am. Soc. Mass Spectrom. doi: 10.1016/j.jasms.2008.11.010 – volume: 874 start-page: 255 year: 1986 ident: ref_15 article-title: A Fourier Transform Infrared Investigation of the Structural Differences between Ribonuclease A and Ribonuclease S publication-title: Biochim. Biophys. Acta doi: 10.1016/0167-4838(86)90024-5 – volume: 382 start-page: 121 year: 2004 ident: ref_20 article-title: Conformational Changes in Gastric H+/K+-ATPase Monitored by Difference Fourier-Transform Infrared Spectroscopy and Hydrogen/Deuterium Exchange publication-title: Biochem. J. doi: 10.1042/BJ20040277 – volume: 37 start-page: 168 year: 2020 ident: ref_68 article-title: Evaluation of Predictors of Protein Relative Stability Obtained by Solid-State Hydrogen/Deuterium Exchange Monitored by FTIR publication-title: Pharm. Res. doi: 10.1007/s11095-020-02897-7 – volume: 271 start-page: 24617 year: 1996 ident: ref_21 article-title: Secondary and Tertiary Structure Changes of Reconstituted P-Glycoprotein. A Fourier Transform Attenuated Total Reflection Infrared Spectroscopy Analysis publication-title: J. Biol. Chem. doi: 10.1074/jbc.271.40.24617 – volume: 30 start-page: 10058 year: 1991 ident: ref_55 article-title: Fourier Transform Infrared Studies of Secondary Structure and Orientation of Pulmonary Surfactant SP-C and Its Effect on the Dynamic Surface Properties of Phospholipids publication-title: Biochemistry doi: 10.1021/bi00105a033 – volume: 1 start-page: 313 year: 1979 ident: ref_75 article-title: Direct Analysis of Continuous Relaxation Spectra publication-title: J. Biochem. Biophys. Methods doi: 10.1016/0165-022X(79)90021-6 – volume: 41 start-page: 15267 year: 2002 ident: ref_42 article-title: Insight into the Factors Influencing the Backbone Dynamics of Three Homologous Proteins, Dendrotoxins I and K, and BPTI: FTIR and Time-Resolved Fluorescence Investigations publication-title: Biochemistry doi: 10.1021/bi0204950 – volume: 16 start-page: 521 year: 1983 ident: ref_59 article-title: Hydrogen Exchange and Structural Dynamics of Proteins and Nucleic Acids publication-title: Q. Rev. Biophys. doi: 10.1017/S0033583500005217 – volume: 142 start-page: 1371 year: 2017 ident: ref_70 article-title: Infrared Imaging of High Density Protein Arrays publication-title: Analyst doi: 10.1039/C6AN02048H – volume: 4 start-page: 1589 year: 1985 ident: ref_54 article-title: Secondary Structure of a Channel-Forming Protein: Porin from E. Coli Outer Membranes publication-title: EMBO J. doi: 10.1002/j.1460-2075.1985.tb03821.x – volume: 257 start-page: 1 year: 1998 ident: ref_46 article-title: Infrared Absorbances of Protein Side Chains publication-title: Anal. Biochem. doi: 10.1006/abio.1997.2502 – volume: 335 start-page: 694 year: 1988 ident: ref_13 article-title: NMR Evidence for an Early Framework Intermediate on the Folding Pathway of Ribonuclease A publication-title: Nature doi: 10.1038/335694a0 – ident: ref_33 doi: 10.1002/9780470027318.a9792 – volume: 111 start-page: 15873 year: 2014 ident: ref_58 article-title: The Nature of Protein Folding Pathways publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1411798111 – volume: 40 start-page: 11876 year: 2001 ident: ref_22 article-title: Structure and Dynamics of the Membrane-Embedded Domain of LmrA Investigated by Coupling Polarized ATR-FTIR Spectroscopy and (1)H/(2)H Exchange publication-title: Biochemistry doi: 10.1021/bi010017+ – volume: 269 start-page: 27409 year: 1994 ident: ref_18 article-title: Tertiary Conformational Changes of the Neurospora Crassa Plasma Membrane H(+)-ATPase Monitored by Hydrogen/Deuterium Exchange Kinetics. A Fourier Transformed Infrared Spectroscopy Approach publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)47000-7 – volume: 100 start-page: 7057 year: 2003 ident: ref_9 article-title: Protein Structure Change Studied by Hydrogen-Deuterium Exchange, Functional Labeling, and Mass Spectrometry publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1232301100 – volume: 261 start-page: 3640 year: 1986 ident: ref_51 article-title: Infrared Spectroscopic Study of Photoreceptor Membrane and Purple Membrane. Protein Secondary Structure and Hydrogen Deuterium Exchange publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)35695-8 – volume: 32 start-page: 372 year: 2014 ident: ref_1 article-title: Therapeutic Protein Aggregation: Mechanisms, Design, and Control publication-title: Trends Biotechnol. doi: 10.1016/j.tibtech.2014.05.005 – volume: 27 start-page: 229 year: 1982 ident: ref_74 article-title: CONTIN: A General Purpose Constrained Regularization Program for Inverting Noisy Linear Algebraic and Integral Equations publication-title: Comput. Phys. Commun. doi: 10.1016/0010-4655(82)90174-6 – volume: 1112 start-page: 62 year: 2020 ident: ref_30 article-title: FTIR Spectroscopy as an Analytical Tool to Compare Glycosylation in Therapeutic Monoclonal Antibodies publication-title: Anal. Chim. Acta doi: 10.1016/j.aca.2020.03.038 – volume: 59 start-page: 1347 year: 2005 ident: ref_64 article-title: Hydrogen-Deuterium Exchange in Bovine Serum Albumin Protein Monitored by Fourier Transform Infrared Spectroscopy, Part I: Structural Studies publication-title: Appl. Spectrosc. doi: 10.1366/000370205774783115 – volume: 336 start-page: 231 year: 2005 ident: ref_24 article-title: Application of the Local Regression Method Interval Partial Least-Squares to the Elucidation of Protein Secondary Structure publication-title: Anal. Biochem. doi: 10.1016/j.ab.2004.10.016 – volume: 95 start-page: 9903 year: 1998 ident: ref_6 article-title: The structural distribution of cooperative interactions in proteins: Analysis of the native state ensemble publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.95.17.9903 – volume: 2 start-page: 104 year: 2009 ident: ref_49 article-title: FTIR Data Processing and Analysis Tools publication-title: Adv. Biomed. Spectrosc. – volume: 94 start-page: 4041 year: 2008 ident: ref_63 article-title: The Kinetics of the Hydrogen/Deuterium Exchange of Epidermal Growth Factor Receptor Ligands publication-title: Biophys. J. doi: 10.1529/biophysj.107.125856 – volume: 1635 start-page: 247 year: 2017 ident: ref_62 article-title: Functional Studies on Membrane Proteins by Means of H/D Exchange in Infrared: Structural Changes in Na + NQR from V. Cholerae in the Presence of Lipids publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-7151-0_13 – volume: 24 start-page: 352 year: 1985 ident: ref_66 article-title: Hydrogen Exchange of Lysozyme Powders. Hydration Dependence of Internal Motions publication-title: Biochemistry doi: 10.1021/bi00323a018 – volume: 74 start-page: 19 year: 2004 ident: ref_16 article-title: Hydrogen-Deuterium Exchange in Membrane Proteins Monitored by IR Spectroscopy: A New Tool to Resolve Protein Structure and Dynamics publication-title: Biopolymers doi: 10.1002/bip.20035 – volume: 233 start-page: 659 year: 1995 ident: ref_53 article-title: A Fourier-Transform Infrared Spectroscopic Investigation of the Hydrogen-Deuterium Exchange and Secondary Structure of the 28-KDa Channel-Forming Integral Membrane Protein (CHIP28) publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1995.659_2.x – volume: 105 start-page: 3269 year: 2016 ident: ref_11 article-title: Rapid Conformational Analysis of Protein Drugs in Formulation by Hydrogen/Deuterium Exchange Mass Spectrometry publication-title: J. Pharm. Sci. doi: 10.1016/j.xphs.2016.07.006 – volume: 24 start-page: 301 year: 1985 ident: ref_73 article-title: Hydrogen-Exchange Evidence for Distinct Structural Classes in Globular Proteins publication-title: Biopolymers doi: 10.1002/bip.360240203 – volume: 93 start-page: 1342 year: 2021 ident: ref_34 article-title: Developability Assessment of an Isolated CH2 Immunoglobulin Domain publication-title: Anal. Chem. doi: 10.1021/acs.analchem.0c02663 – volume: 26 start-page: 5163 year: 1987 ident: ref_57 article-title: Solvent Exchange of Buried Water and Hydrogen Exchange of Peptide NH Groups Hydrogen Bonded to Buried Waters in Bovine Pancreatic Trypsin Inhibitor publication-title: Biochemistry doi: 10.1021/bi00390a040 – volume: 272 start-page: 262 year: 1997 ident: ref_19 article-title: Fourier Transform Infrared Spectroscopy Study of the Secondary Structure of the Gastric H+,K+-ATPase and of Its Membrane-Associated Proteolytic Peptides publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.1.262 – volume: 29 start-page: 9185 year: 1990 ident: ref_26 article-title: Determination of Protein Secondary Structure Using Factor Analysis of Infrared Spectra publication-title: Biochemistry doi: 10.1021/bi00491a012 – volume: 121 start-page: 5115 year: 1999 ident: ref_65 article-title: Hydrogen-Deuterium Exchange of Streptavidin and Its Complex with Biotin Studied by 2D-Attenuated Total Reflection Fourier Transform Infrared Spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja984208k – volume: 92 start-page: 6486 year: 2020 ident: ref_5 article-title: Complete Extraction of Protein Dynamics Information in Hydrogen/Deuterium Exchange Mass Spectrometry Data publication-title: Anal. Chem. doi: 10.1021/acs.analchem.9b05724 – volume: 21 start-page: 987 year: 2012 ident: ref_60 article-title: Protein Hydrogen Exchange: Testing Current Models publication-title: Protein Sci. doi: 10.1002/pro.2082 – volume: 2 start-page: 522 year: 1993 ident: ref_8 article-title: Determination of Amide Hydrogen Exchange by Mass Spectrometry: A New Tool for Protein Structure Elucidation publication-title: Protein Sci. doi: 10.1002/pro.5560020404 – ident: ref_2 doi: 10.1371/journal.pone.0176748 – volume: 1767 start-page: 1073 year: 2007 ident: ref_45 article-title: Infrared Spectroscopy of Proteins publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbabio.2007.06.004 – volume: 11 start-page: 527 year: 2012 ident: ref_4 article-title: Analytical Tools for Characterizing Biopharmaceuticals and the Implications for Biosimilars publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd3746 – volume: 103 start-page: 223 year: 2018 ident: ref_14 article-title: Ultraviolet Resonance Raman Spectroscopic Markers for Protein Structure and Dynamics publication-title: Trends Anal. Chem. doi: 10.1016/j.trac.2017.12.002 – volume: 18 start-page: 1864 year: 2020 ident: ref_40 article-title: A Convenient Protein Library for Spectroscopic Calibrations publication-title: Comput. Struct. Biotechnol. J. doi: 10.1016/j.csbj.2020.07.001 |
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| SubjectTerms | Biological research Biology, Experimental Chemical reactions Conformation Deuterium Exchange Measurement - methods Experiments Fourier transform infrared spectroscopy Fourier transforms Hydrogen - chemistry Ligands Mass spectrometry NMR Nuclear magnetic resonance Protein Array Analysis - methods Proteins Proteins - chemistry Scientific imaging Spectroscopy, Fourier Transform Infrared - methods |
| Title | Protein Microarrays for High Throughput Hydrogen/Deuterium Exchange Monitored by FTIR Imaging |
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