Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins

Fluorescence anisotropy kinetics were employed to quantify the nanosecond mobility of tryptophan residues in different conformational states (native, molten globule, unfolded) of apomyoglobins. Of particular interest is the similarity between the fluorescence anisotropy decays of tryptophans in the...

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Veröffentlicht in:	Biochemistry (Easton) 2000-02, Vol.39 (7), p.1879-1889
Hauptverfasser:	Tcherkasskaya, Olga, Ptitsyn, Oleg B, Knutson, Jay R
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Apoproteins - chemistry Diffusion Fluorescence Polarization - methods Horses Kinetics Myoglobin - chemistry Protein Conformation Protein Folding Spectrometry, Fluorescence Thermodynamics Time Factors Tryptophan - chemistry Tuna Whales
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container_title	Biochemistry (Easton)
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creator	Tcherkasskaya, Olga Ptitsyn, Oleg B Knutson, Jay R
description	Fluorescence anisotropy kinetics were employed to quantify the nanosecond mobility of tryptophan residues in different conformational states (native, molten globule, unfolded) of apomyoglobins. Of particular interest is the similarity between the fluorescence anisotropy decays of tryptophans in the native and molten globule states. We find that, in these compact states, tryptophan residues rotate rapidly within a cone of semiangle 22−25° and a correlation time of 0.5 ns, in addition to rotating together with the whole protein with a correlation time of 7−11 ns. The similar nanosecond dynamics of tryptophan residues in both states suggests that the conformation changes that distinguish the molten globule and native states of apomyoglobins originate from either subtle, slow rearrangements or fast changes distant from these tryptophans.
doi_str_mv	10.1021/bi992117+
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The similar nanosecond dynamics of tryptophan residues in both states suggests that the conformation changes that distinguish the molten globule and native states of apomyoglobins originate from either subtle, slow rearrangements or fast changes distant from these tryptophans.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi992117+</identifier><identifier>PMID: 10677239</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Apoproteins - chemistry ; Diffusion ; Fluorescence Polarization - methods ; Horses ; Kinetics ; Myoglobin - chemistry ; Protein Conformation ; Protein Folding ; Spectrometry, Fluorescence ; Thermodynamics ; Time Factors ; Tryptophan - chemistry ; Tuna ; Whales</subject><ispartof>Biochemistry (Easton), 2000-02, Vol.39 (7), p.1879-1889</ispartof><rights>Copyright © 2000 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a346t-44682299c0645a5c03d4f1b7da3ad52986c51380121506e7e81abee7cb05c1823</citedby><cites>FETCH-LOGICAL-a346t-44682299c0645a5c03d4f1b7da3ad52986c51380121506e7e81abee7cb05c1823</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi992117+$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi992117+$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27055,27903,27904,56716,56766</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10677239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tcherkasskaya, Olga</creatorcontrib><creatorcontrib>Ptitsyn, Oleg B</creatorcontrib><creatorcontrib>Knutson, Jay R</creatorcontrib><title>Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Fluorescence anisotropy kinetics were employed to quantify the nanosecond mobility of tryptophan residues in different conformational states (native, molten globule, unfolded) of apomyoglobins. 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The similar nanosecond dynamics of tryptophan residues in both states suggests that the conformation changes that distinguish the molten globule and native states of apomyoglobins originate from either subtle, slow rearrangements or fast changes distant from these tryptophans.</description><subject>Animals</subject><subject>Apoproteins - chemistry</subject><subject>Diffusion</subject><subject>Fluorescence Polarization - methods</subject><subject>Horses</subject><subject>Kinetics</subject><subject>Myoglobin - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Spectrometry, Fluorescence</subject><subject>Thermodynamics</subject><subject>Time Factors</subject><subject>Tryptophan - chemistry</subject><subject>Tuna</subject><subject>Whales</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpl0FFLHDEQB_BQFD2vPvQLyD6ICGXbSXaTbB7ltFU47FFP-taQzWY1djdZkxx4375rV6Xg0zDMb2bgj9AnDF8wEPy1tkIQjPnnD2iGKYG8FILuoBkAsJwIBvvoIMaHsS2Bl3toHwPjnBRihn5fK-ej0d412fnWqd7qmPk2W4ftkPxwr1zMrMvObduaYFzKFt61PvQqWe9Ul90klcy_jbPB91t_1_l69Kvgk7EufkS7reqiOXypc3T77WK9uMyXP75fLc6WuSpKlvKyZBUhQmhgJVVUQ9GULa55owrVUCIqpikuKsAEU2CGmwqr2hiua6AaV6SYo5Pp7hD848bEJHsbtek65YzfRMlBYKC4GuHpBHXwMQbTyiHYXoWtxCCfw5SvYY706OXmpu5N8x-cwhtBPgEbk3l6m6vwRzJecCrXqxt5Xf0kv3i1ksXojyevdJQPfhPGAOP7v38B3u2JYg</recordid><startdate>20000222</startdate><enddate>20000222</enddate><creator>Tcherkasskaya, Olga</creator><creator>Ptitsyn, Oleg B</creator><creator>Knutson, Jay R</creator><general>American Chemical Society</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>7X8</scope></search><sort><creationdate>20000222</creationdate><title>Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins</title><author>Tcherkasskaya, Olga ; Ptitsyn, Oleg B ; Knutson, Jay R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a346t-44682299c0645a5c03d4f1b7da3ad52986c51380121506e7e81abee7cb05c1823</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Animals</topic><topic>Apoproteins - chemistry</topic><topic>Diffusion</topic><topic>Fluorescence Polarization - methods</topic><topic>Horses</topic><topic>Kinetics</topic><topic>Myoglobin - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Spectrometry, Fluorescence</topic><topic>Thermodynamics</topic><topic>Time Factors</topic><topic>Tryptophan - chemistry</topic><topic>Tuna</topic><topic>Whales</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tcherkasskaya, Olga</creatorcontrib><creatorcontrib>Ptitsyn, Oleg B</creatorcontrib><creatorcontrib>Knutson, Jay R</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tcherkasskaya, Olga</au><au>Ptitsyn, Oleg B</au><au>Knutson, Jay R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2000-02-22</date><risdate>2000</risdate><volume>39</volume><issue>7</issue><spage>1879</spage><epage>1889</epage><pages>1879-1889</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>Fluorescence anisotropy kinetics were employed to quantify the nanosecond mobility of tryptophan residues in different conformational states (native, molten globule, unfolded) of apomyoglobins. 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subjects	Animals Apoproteins - chemistry Diffusion Fluorescence Polarization - methods Horses Kinetics Myoglobin - chemistry Protein Conformation Protein Folding Spectrometry, Fluorescence Thermodynamics Time Factors Tryptophan - chemistry Tuna Whales
title	Nanosecond Dynamics of Tryptophans in Different Conformational States of Apomyoglobin Proteins
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