Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich
The relationship of a protein structure obtained by crystallography to the in vivo solution structure is of great interest in the study of protein structure and function. Upon crystallization the structure of a protein molecule may change due to crystal lattice forces and different hydration levels....
Gespeichert in:
| Veröffentlicht in: | Journal of the American Chemical Society 1985-05, Vol.107 (11), p.3350-3352 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3352 |
|---|---|
| container_issue | 11 |
| container_start_page | 3350 |
| container_title | Journal of the American Chemical Society |
| container_volume | 107 |
| creator | Potter, William T Houtchens, Robert A Caughey, Winslow S |
| description | The relationship of a protein structure obtained by crystallography to the in vivo solution structure is of great interest in the study of protein structure and function. Upon crystallization the structure of a protein molecule may change due to crystal lattice forces and different hydration levels. With hemeprotein ligand infrared spectra can provide a sensitive probe for monitoring ligand site structures in both crystals and solutions. The spectra for CO, CN super(-), N sub(3) super(-), NO, and O sub(2) as ligands have been observed for several hemeproteins in solution and provide evidence the multiple ligand site structures (conformers) are present. |
| doi_str_mv | 10.1021/ja00297a053 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_14392501</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>14392501</sourcerecordid><originalsourceid>FETCH-LOGICAL-a361t-6fc24840b5322e99fd505dd0ca0ef6581e349ebc312578ee3bbd7c99903154013</originalsourceid><addsrcrecordid>eNpt0M2O0zAQB3ALgURZOPECPiA4oIA_4iQ-LtXuglQJJMqFi-U4k9YlsYvHQVuegwfG0NWKA6exNT-PPH9CnnP2hjPB3x4sY0K3lin5gKy4EqxSXDQPyYqVRtV2jXxMniAeyrUWHV-RX-t0wmynyf-02cdQ-TAsDgbq9jbsAKkP9JhihlIxp8XlJQGNPUL6UVR_KmBMNpUzHsHlFNHF44nGkTqb-hjoHEO89QPQye9sGArMke6X2Qa6hznuptj7gPSSlib9uiTv9k_Jo9FOCM_u6gX5cn21Xb-vNh9vPqwvN5WVDc9VMzpRdzXrlRQCtB4HxdQwMGcZjI3qOMhaQ-8kF6rtAGTfD63TWjPJVc24vCAvz3PLht8XwGxmjw6myQaICxpeSy3UX_j6DF3ZDxOM5pj8bNPJcGb-JG_-Sb7oF3djLTo7lXiC83j_pFOa1aorrDozjxlu79s2fTNNK1tltp8-G7W55utt_c7cFP_q7K1Dc4hLCiWb_37gN3C7oZg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>14392501</pqid></control><display><type>article</type><title>Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich</title><source>ACS Publications</source><creator>Potter, William T ; Houtchens, Robert A ; Caughey, Winslow S</creator><creatorcontrib>Potter, William T ; Houtchens, Robert A ; Caughey, Winslow S</creatorcontrib><description>The relationship of a protein structure obtained by crystallography to the in vivo solution structure is of great interest in the study of protein structure and function. Upon crystallization the structure of a protein molecule may change due to crystal lattice forces and different hydration levels. With hemeprotein ligand infrared spectra can provide a sensitive probe for monitoring ligand site structures in both crystals and solutions. The spectra for CO, CN super(-), N sub(3) super(-), NO, and O sub(2) as ligands have been observed for several hemeproteins in solution and provide evidence the multiple ligand site structures (conformers) are present.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja00297a053</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Biological and medical sciences ; carbon monoxide ; Fundamental and applied biological sciences. Psychology ; hemoglobin A ; hemoglobin Zurich ; I.R. spectroscopy ; man ; Molecular biophysics ; Spectroscopy : techniques and spectras</subject><ispartof>Journal of the American Chemical Society, 1985-05, Vol.107 (11), p.3350-3352</ispartof><rights>1986 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a361t-6fc24840b5322e99fd505dd0ca0ef6581e349ebc312578ee3bbd7c99903154013</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja00297a053$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja00297a053$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,777,781,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8590458$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Potter, William T</creatorcontrib><creatorcontrib>Houtchens, Robert A</creatorcontrib><creatorcontrib>Caughey, Winslow S</creatorcontrib><title>Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>The relationship of a protein structure obtained by crystallography to the in vivo solution structure is of great interest in the study of protein structure and function. Upon crystallization the structure of a protein molecule may change due to crystal lattice forces and different hydration levels. With hemeprotein ligand infrared spectra can provide a sensitive probe for monitoring ligand site structures in both crystals and solutions. The spectra for CO, CN super(-), N sub(3) super(-), NO, and O sub(2) as ligands have been observed for several hemeproteins in solution and provide evidence the multiple ligand site structures (conformers) are present.</description><subject>Biological and medical sciences</subject><subject>carbon monoxide</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>hemoglobin A</subject><subject>hemoglobin Zurich</subject><subject>I.R. spectroscopy</subject><subject>man</subject><subject>Molecular biophysics</subject><subject>Spectroscopy : techniques and spectras</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1985</creationdate><recordtype>article</recordtype><recordid>eNpt0M2O0zAQB3ALgURZOPECPiA4oIA_4iQ-LtXuglQJJMqFi-U4k9YlsYvHQVuegwfG0NWKA6exNT-PPH9CnnP2hjPB3x4sY0K3lin5gKy4EqxSXDQPyYqVRtV2jXxMniAeyrUWHV-RX-t0wmynyf-02cdQ-TAsDgbq9jbsAKkP9JhihlIxp8XlJQGNPUL6UVR_KmBMNpUzHsHlFNHF44nGkTqb-hjoHEO89QPQye9sGArMke6X2Qa6hznuptj7gPSSlib9uiTv9k_Jo9FOCM_u6gX5cn21Xb-vNh9vPqwvN5WVDc9VMzpRdzXrlRQCtB4HxdQwMGcZjI3qOMhaQ-8kF6rtAGTfD63TWjPJVc24vCAvz3PLht8XwGxmjw6myQaICxpeSy3UX_j6DF3ZDxOM5pj8bNPJcGb-JG_-Sb7oF3djLTo7lXiC83j_pFOa1aorrDozjxlu79s2fTNNK1tltp8-G7W55utt_c7cFP_q7K1Dc4hLCiWb_37gN3C7oZg</recordid><startdate>19850501</startdate><enddate>19850501</enddate><creator>Potter, William T</creator><creator>Houtchens, Robert A</creator><creator>Caughey, Winslow S</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19850501</creationdate><title>Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich</title><author>Potter, William T ; Houtchens, Robert A ; Caughey, Winslow S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a361t-6fc24840b5322e99fd505dd0ca0ef6581e349ebc312578ee3bbd7c99903154013</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1985</creationdate><topic>Biological and medical sciences</topic><topic>carbon monoxide</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>hemoglobin A</topic><topic>hemoglobin Zurich</topic><topic>I.R. spectroscopy</topic><topic>man</topic><topic>Molecular biophysics</topic><topic>Spectroscopy : techniques and spectras</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Potter, William T</creatorcontrib><creatorcontrib>Houtchens, Robert A</creatorcontrib><creatorcontrib>Caughey, Winslow S</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Potter, William T</au><au>Houtchens, Robert A</au><au>Caughey, Winslow S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>1985-05-01</date><risdate>1985</risdate><volume>107</volume><issue>11</issue><spage>3350</spage><epage>3352</epage><pages>3350-3352</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The relationship of a protein structure obtained by crystallography to the in vivo solution structure is of great interest in the study of protein structure and function. Upon crystallization the structure of a protein molecule may change due to crystal lattice forces and different hydration levels. With hemeprotein ligand infrared spectra can provide a sensitive probe for monitoring ligand site structures in both crystals and solutions. The spectra for CO, CN super(-), N sub(3) super(-), NO, and O sub(2) as ligands have been observed for several hemeproteins in solution and provide evidence the multiple ligand site structures (conformers) are present.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/ja00297a053</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0002-7863 |
| ispartof | Journal of the American Chemical Society, 1985-05, Vol.107 (11), p.3350-3352 |
| issn | 0002-7863 1520-5126 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_14392501 |
| source | ACS Publications |
| subjects | Biological and medical sciences carbon monoxide Fundamental and applied biological sciences. Psychology hemoglobin A hemoglobin Zurich I.R. spectroscopy man Molecular biophysics Spectroscopy : techniques and spectras |
| title | Crystallization-induced changes in protein structure observed by infrared spectroscopy of carbon monoxide liganded to human hemoglobins A and Zurich |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T20%3A46%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystallization-induced%20changes%20in%20protein%20structure%20observed%20by%20infrared%20spectroscopy%20of%20carbon%20monoxide%20liganded%20to%20human%20hemoglobins%20A%20and%20Zurich&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Potter,%20William%20T&rft.date=1985-05-01&rft.volume=107&rft.issue=11&rft.spage=3350&rft.epage=3352&rft.pages=3350-3352&rft.issn=0002-7863&rft.eissn=1520-5126&rft.coden=JACSAT&rft_id=info:doi/10.1021/ja00297a053&rft_dat=%3Cproquest_cross%3E14392501%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=14392501&rft_id=info:pmid/&rfr_iscdi=true |