THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins

THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins

The activity of enzymes in organic solvents substantially increases in the presence of crown ethers. Tris(hydroxymethyl)aminomethane (tris) is chosen as a model compound to simulate the interaction of surface amino groups of proteins with crown ether. The methods of FTIR and time-domain THz spectros...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of spectroscopy (Hindawi) 2012-01, Vol.2012 (2012), p.1-4
Hauptverfasser: Shkurinov, A. P., Nazarov, M. M., Mankova, A. A., Chikishev, A. Yu, Brandt, N. N., Sakodynskaya, I. K.
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 4
container_issue 2012
container_start_page 1
container_title Journal of spectroscopy (Hindawi)
container_volume 2012
creator Shkurinov, A. P.
Nazarov, M. M.
Mankova, A. A.
Chikishev, A. Yu
Brandt, N. N.
Sakodynskaya, I. K.
description The activity of enzymes in organic solvents substantially increases in the presence of crown ethers. Tris(hydroxymethyl)aminomethane (tris) is chosen as a model compound to simulate the interaction of surface amino groups of proteins with crown ether. The methods of FTIR and time-domain THz spectroscopy are used to study the interaction of tris with 18-crown-6. The THz spectra of the complexes are measured for the first time.
doi_str_mv 10.1155/2012/745136
format Article
fullrecord <record><control><sourceid>emarefa_cross</sourceid><recordid>TN_cdi_crossref_primary_10_1155_2012_745136</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>998788</sourcerecordid><originalsourceid>FETCH-LOGICAL-c327t-dd5c8bf33fb477bf3f3f37515faeda9cfa7cedc3e8431b4fe24a8c0c2ac247dd3</originalsourceid><addsrcrecordid>eNqFkM1Lw0AQxRdRsNSePAt7VmL3002OUqwtVJSmnsN2d9ampEnZ3SD1rzch0qvMYd4MPx68h9AtJY-USjllhLKpEpLypws0YpyKRGQ8uzxrRq7RJIQ9IYRKwUQmR2i_WfxgXVu8XOP8CCb6JpjmeMKNw29NBaattMf5KUQ4BLzZ6Yjz8tA9I-B5W5tYNnWyhv62OI--NbH1usKzna6_IPQ2H76JUNbhBl05XQWY_O0x-py_bGaLZPX-upw9rxLDmYqJtdKkW8e52wqlOtGPklQ6DVZnxmllwBoOqeB0KxwwoVNDDNOGCWUtH6OHwdd0WYIHVxx9edD-VFBS9E0VfVPF0FRH3w_0rqyt_i7_ge8GGDoEnD7DWZaqNOW_q3t0Og</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins</title><source>DOAJ Directory of Open Access Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Wiley Online Library (Open Access Collection)</source><source>Alma/SFX Local Collection</source><creator>Shkurinov, A. P. ; Nazarov, M. M. ; Mankova, A. A. ; Chikishev, A. Yu ; Brandt, N. N. ; Sakodynskaya, I. K.</creator><creatorcontrib>Shkurinov, A. P. ; Nazarov, M. M. ; Mankova, A. A. ; Chikishev, A. Yu ; Brandt, N. N. ; Sakodynskaya, I. K.</creatorcontrib><description>The activity of enzymes in organic solvents substantially increases in the presence of crown ethers. Tris(hydroxymethyl)aminomethane (tris) is chosen as a model compound to simulate the interaction of surface amino groups of proteins with crown ether. The methods of FTIR and time-domain THz spectroscopy are used to study the interaction of tris with 18-crown-6. The THz spectra of the complexes are measured for the first time.</description><identifier>ISSN: 2314-4920</identifier><identifier>ISSN: 0712-4813</identifier><identifier>EISSN: 2314-4939</identifier><identifier>EISSN: 1875-922X</identifier><identifier>DOI: 10.1155/2012/745136</identifier><language>eng</language><publisher>Cairo, Egypt: Hindawi Publishing Corporation</publisher><ispartof>Journal of spectroscopy (Hindawi), 2012-01, Vol.2012 (2012), p.1-4</ispartof><rights>Copyright © 2012 N. N. Brandt et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c327t-dd5c8bf33fb477bf3f3f37515faeda9cfa7cedc3e8431b4fe24a8c0c2ac247dd3</citedby><cites>FETCH-LOGICAL-c327t-dd5c8bf33fb477bf3f3f37515faeda9cfa7cedc3e8431b4fe24a8c0c2ac247dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,865,27928,27929</link.rule.ids></links><search><creatorcontrib>Shkurinov, A. P.</creatorcontrib><creatorcontrib>Nazarov, M. M.</creatorcontrib><creatorcontrib>Mankova, A. A.</creatorcontrib><creatorcontrib>Chikishev, A. Yu</creatorcontrib><creatorcontrib>Brandt, N. N.</creatorcontrib><creatorcontrib>Sakodynskaya, I. K.</creatorcontrib><title>THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins</title><title>Journal of spectroscopy (Hindawi)</title><description>The activity of enzymes in organic solvents substantially increases in the presence of crown ethers. Tris(hydroxymethyl)aminomethane (tris) is chosen as a model compound to simulate the interaction of surface amino groups of proteins with crown ether. The methods of FTIR and time-domain THz spectroscopy are used to study the interaction of tris with 18-crown-6. The THz spectra of the complexes are measured for the first time.</description><issn>2314-4920</issn><issn>0712-4813</issn><issn>2314-4939</issn><issn>1875-922X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>RHX</sourceid><recordid>eNqFkM1Lw0AQxRdRsNSePAt7VmL3002OUqwtVJSmnsN2d9ampEnZ3SD1rzch0qvMYd4MPx68h9AtJY-USjllhLKpEpLypws0YpyKRGQ8uzxrRq7RJIQ9IYRKwUQmR2i_WfxgXVu8XOP8CCb6JpjmeMKNw29NBaattMf5KUQ4BLzZ6Yjz8tA9I-B5W5tYNnWyhv62OI--NbH1usKzna6_IPQ2H76JUNbhBl05XQWY_O0x-py_bGaLZPX-upw9rxLDmYqJtdKkW8e52wqlOtGPklQ6DVZnxmllwBoOqeB0KxwwoVNDDNOGCWUtH6OHwdd0WYIHVxx9edD-VFBS9E0VfVPF0FRH3w_0rqyt_i7_ge8GGDoEnD7DWZaqNOW_q3t0Og</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Shkurinov, A. P.</creator><creator>Nazarov, M. M.</creator><creator>Mankova, A. A.</creator><creator>Chikishev, A. Yu</creator><creator>Brandt, N. N.</creator><creator>Sakodynskaya, I. K.</creator><general>Hindawi Publishing Corporation</general><scope>ADJCN</scope><scope>AHFXO</scope><scope>RHU</scope><scope>RHW</scope><scope>RHX</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20120101</creationdate><title>THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins</title><author>Shkurinov, A. P. ; Nazarov, M. M. ; Mankova, A. A. ; Chikishev, A. Yu ; Brandt, N. N. ; Sakodynskaya, I. K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c327t-dd5c8bf33fb477bf3f3f37515faeda9cfa7cedc3e8431b4fe24a8c0c2ac247dd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shkurinov, A. P.</creatorcontrib><creatorcontrib>Nazarov, M. M.</creatorcontrib><creatorcontrib>Mankova, A. A.</creatorcontrib><creatorcontrib>Chikishev, A. Yu</creatorcontrib><creatorcontrib>Brandt, N. N.</creatorcontrib><creatorcontrib>Sakodynskaya, I. K.</creatorcontrib><collection>الدوريات العلمية والإحصائية - e-Marefa Academic and Statistical Periodicals</collection><collection>معرفة - المحتوى العربي الأكاديمي المتكامل - e-Marefa Academic Complete</collection><collection>Hindawi Publishing Complete</collection><collection>Hindawi Publishing Subscription Journals</collection><collection>Hindawi Publishing Open Access</collection><collection>CrossRef</collection><jtitle>Journal of spectroscopy (Hindawi)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shkurinov, A. P.</au><au>Nazarov, M. M.</au><au>Mankova, A. A.</au><au>Chikishev, A. Yu</au><au>Brandt, N. N.</au><au>Sakodynskaya, I. K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins</atitle><jtitle>Journal of spectroscopy (Hindawi)</jtitle><date>2012-01-01</date><risdate>2012</risdate><volume>2012</volume><issue>2012</issue><spage>1</spage><epage>4</epage><pages>1-4</pages><issn>2314-4920</issn><issn>0712-4813</issn><eissn>2314-4939</eissn><eissn>1875-922X</eissn><abstract>The activity of enzymes in organic solvents substantially increases in the presence of crown ethers. Tris(hydroxymethyl)aminomethane (tris) is chosen as a model compound to simulate the interaction of surface amino groups of proteins with crown ether. The methods of FTIR and time-domain THz spectroscopy are used to study the interaction of tris with 18-crown-6. The THz spectra of the complexes are measured for the first time.</abstract><cop>Cairo, Egypt</cop><pub>Hindawi Publishing Corporation</pub><doi>10.1155/2012/745136</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2314-4920
ispartof Journal of spectroscopy (Hindawi), 2012-01, Vol.2012 (2012), p.1-4
issn 2314-4920
0712-4813
2314-4939
1875-922X
language eng
recordid cdi_crossref_primary_10_1155_2012_745136
source DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; Wiley Online Library (Open Access Collection); Alma/SFX Local Collection
title THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-16T14%3A11%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-emarefa_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=THz%20and%20IR%20Spectroscopy%20of%20Molecular%20Systems%20That%20Simulate%20Function-Related%20Structural%20Changes%20of%20Proteins&rft.jtitle=Journal%20of%20spectroscopy%20(Hindawi)&rft.au=Shkurinov,%20A.%20P.&rft.date=2012-01-01&rft.volume=2012&rft.issue=2012&rft.spage=1&rft.epage=4&rft.pages=1-4&rft.issn=2314-4920&rft.eissn=2314-4939&rft_id=info:doi/10.1155/2012/745136&rft_dat=%3Cemarefa_cross%3E998788%3C/emarefa_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true