Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics
As more and more high‐resolution structures of proteins become available, the new challenge is the understanding of these small conformational changes that are responsible for protein activity. Specialized difference Fourier transform infrared (FTIR) techniques allow the recording of side‐chain modi...
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| Veröffentlicht in: | Biopolymers 2004-05, Vol.74 (1-2), p.19-26 |
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| creator | Vigano, C. Smeyers, M. Raussens, V. Scheirlinckx, F. Ruysschaert, J.M. Goormaghtigh, E. |
| description | As more and more high‐resolution structures of proteins become available, the new challenge is the understanding of these small conformational changes that are responsible for protein activity. Specialized difference Fourier transform infrared (FTIR) techniques allow the recording of side‐chain modifications or minute secondary structure changes. Yet, large domain movements remain usually unnoticed. FTIR spectroscopy provides a unique opportunity to record 1H/2H exchange kinetics at the level of the amide proton. This approach is extremely sensitive to tertiary structure changes and yields quantitative data on domain/domain interactions. An experimental setup designed for attenuated total reflection and a specific approach for the analysis of the results is described. The study of one membrane protein, the gastric H+,K+‐ATPase, demonstrates the usefulness of 1H/2H exchange kinetics for the understanding of the molecular movement related to the catalytic activity. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004 |
| doi_str_mv | 10.1002/bip.20035 |
| format | Article |
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Specialized difference Fourier transform infrared (FTIR) techniques allow the recording of side‐chain modifications or minute secondary structure changes. Yet, large domain movements remain usually unnoticed. FTIR spectroscopy provides a unique opportunity to record 1H/2H exchange kinetics at the level of the amide proton. This approach is extremely sensitive to tertiary structure changes and yields quantitative data on domain/domain interactions. An experimental setup designed for attenuated total reflection and a specific approach for the analysis of the results is described. The study of one membrane protein, the gastric H+,K+‐ATPase, demonstrates the usefulness of 1H/2H exchange kinetics for the understanding of the molecular movement related to the catalytic activity. © 2004 Wiley Periodicals, Inc. 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Biopolymers, 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3905-cbed2467dc610e8f449aa56647c1dcbc3a62ec0b806962fae00c4486bdb78f263</citedby><cites>FETCH-LOGICAL-c3905-cbed2467dc610e8f449aa56647c1dcbc3a62ec0b806962fae00c4486bdb78f263</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.20035$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.20035$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15137087$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vigano, C.</creatorcontrib><creatorcontrib>Smeyers, M.</creatorcontrib><creatorcontrib>Raussens, V.</creatorcontrib><creatorcontrib>Scheirlinckx, F.</creatorcontrib><creatorcontrib>Ruysschaert, J.M.</creatorcontrib><creatorcontrib>Goormaghtigh, E.</creatorcontrib><title>Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics</title><title>Biopolymers</title><addtitle>Biopolymers</addtitle><description>As more and more high‐resolution structures of proteins become available, the new challenge is the understanding of these small conformational changes that are responsible for protein activity. Specialized difference Fourier transform infrared (FTIR) techniques allow the recording of side‐chain modifications or minute secondary structure changes. Yet, large domain movements remain usually unnoticed. FTIR spectroscopy provides a unique opportunity to record 1H/2H exchange kinetics at the level of the amide proton. This approach is extremely sensitive to tertiary structure changes and yields quantitative data on domain/domain interactions. An experimental setup designed for attenuated total reflection and a specific approach for the analysis of the results is described. The study of one membrane protein, the gastric H+,K+‐ATPase, demonstrates the usefulness of 1H/2H exchange kinetics for the understanding of the molecular movement related to the catalytic activity. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004</description><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>amide proton</subject><subject>attenuated total reflection</subject><subject>Calorimetry</subject><subject>Catalysis</subject><subject>Cell Membrane - metabolism</subject><subject>Deuterium</subject><subject>Fourier transform infrared</subject><subject>H(+)-K(+)-Exchanging ATPase - chemistry</subject><subject>Hydrogen</subject><subject>hydrogen deuterium exchange</subject><subject>Kinetics</subject><subject>membrane proteins</subject><subject>Models, Chemical</subject><subject>Models, Statistical</subject><subject>Normal Distribution</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Protons</subject><subject>Spectrophotometry, Infrared - methods</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><subject>Stomach - enzymology</subject><subject>Time Factors</subject><subject>Water</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1TAQhS0EopfCgj-AvEJikXbsJHbCrg_ae6HipSIkNpZjT4ohsYOd0GbNHydwL2WF2MxsvnM0Zw4hjxkcMAB-2LjhgAPk5R2yYlDLDHjF75IVAIgsL3m5Rx6k9AWgKHIG98keK1kuoZIr8mM92xiu0GcWpxGjm3qKN-az9ldInac99k3UHukQw4jOJ9oH78YQ0dJmppv3NA1oxhiSCcP8nB5Rj9d0DKFbBo2YQvf9VkzTGCczThGp9pba2evemfSQ3Gt1l_DRbu-TD2cvLk_W2cWb883J0UVm8hrKzDRoeSGkNYIBVm1R1FqXQhTSMGsak2vB0UBTgagFbzUCmKKoRGMbWbVc5Pvk6dZ3OefbhGlUvUsGu27JF6akJKsZcCH_CzJZVUXFywV8tgXN8oAUsVVDdL2Os2KgflWjlmrU72oW9snOdGp6tH_JXRcLcLgFrl2H87-d1PHm7R_LbKtwacSbW4WOX9WSQpbq4-tzdXb57tXpp_VLdZr_BCMqqh8</recordid><startdate>20040501</startdate><enddate>20040501</enddate><creator>Vigano, C.</creator><creator>Smeyers, M.</creator><creator>Raussens, V.</creator><creator>Scheirlinckx, F.</creator><creator>Ruysschaert, J.M.</creator><creator>Goormaghtigh, E.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20040501</creationdate><title>Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics</title><author>Vigano, C. ; 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| subjects | Adenosine Triphosphatases - chemistry Adenosine Triphosphate - chemistry amide proton attenuated total reflection Calorimetry Catalysis Cell Membrane - metabolism Deuterium Fourier transform infrared H(+)-K(+)-Exchanging ATPase - chemistry Hydrogen hydrogen deuterium exchange Kinetics membrane proteins Models, Chemical Models, Statistical Normal Distribution Phosphorylation Protein Binding Protein Conformation Protein Structure, Tertiary Protons Spectrophotometry, Infrared - methods Spectroscopy, Fourier Transform Infrared Stomach - enzymology Time Factors Water |
| title | Hydrogen-deuterium exchange in membrane proteins monitored by IR spectroscopy: A new tool to resolve protein structure and dynamics |
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