Loading…
Laser Raman scattering. A molecular probe of the contractile state of intact single muscle fibers
The 500 to 1,800-cm-1 region of the Raman spectra of intact single muscle fibers from the giant barnacle are dominated by bands caused by the protein component of the fibers. The frequency and the intensity of the conformationally sensitive bands indicate that the contractile proteins adopt a predom...
Saved in:
Published in: | Biophysical journal 1980-07, Vol.31 (1), p.1-8 |
---|---|
Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c530t-ba2812f8f9dbf4db0bd8b2508dafe52141cbc8b57c64f887423a92977db722a53 |
---|---|
cites | |
container_end_page | 8 |
container_issue | 1 |
container_start_page | 1 |
container_title | Biophysical journal |
container_volume | 31 |
creator | Pézolet, M. Pigeon-Gosselin, M. Nadeau, J. Caillé, J.P. |
description | The 500 to 1,800-cm-1 region of the Raman spectra of intact single muscle fibers from the giant barnacle are dominated by bands caused by the protein component of the fibers. The frequency and the intensity of the conformationally sensitive bands indicate that the contractile proteins adopt a predominantly alpha-helical structure and are not affected when the contractile state of the fibers is changed from relaxed to contracted by addition of ATP and Ca. However, the contraction induces a decrease of the scattering intensity of some of the Raman bands caused by the acidic and tryptophan side chains, showing that these amino acids are involved during the generation of tension. |
doi_str_mv | 10.1016/S0006-3495(80)85036-3 |
format | article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1328760</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349580850363</els_id><sourcerecordid>75541624</sourcerecordid><originalsourceid>FETCH-LOGICAL-c530t-ba2812f8f9dbf4db0bd8b2508dafe52141cbc8b57c64f887423a92977db722a53</originalsourceid><addsrcrecordid>eNqFUctqHDEQFCHG2Tj5BINOITmMLWmkkfZiY0wehgWDnZyFpGnZCjOjtaQx5O-tfbDEJ5-a7qrqLroQOqXkjBLand8TQrqm5UvxVZFvSpC2du_QggrOGkJU9x4tDpQP6GPOfwmhTBB6jI4lk4wztUBmZTIkfGdGM-HsTCmQwvRwhq_wGAdw82ASXqdoAUePyyNgF6eSjCthAJyLKVsgTKWOcK7SOh7n7GrxwULKn9CRN0OGz_t6gv78-P77-lezuv15c321apxoSWmsYYoyr_yyt573lthe2epW9caDYJRTZ52yQrqOe6UkZ61ZsqWUvZWMGdGeoIvd3vVsR-gdbGwOep3CaNI_HU3Qr5EpPOqH-Kxpy5TsSF3wZb8gxacZctFjyA6GwUwQ56ylEJx2jFei2BFdijkn8IcjlOhNNnqbjd48Xiuit9notupO_3d4UO3DqPjlDof6pucASWcXYHLQhwSu6D6GNy68AILaoII</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>75541624</pqid></control><display><type>article</type><title>Laser Raman scattering. A molecular probe of the contractile state of intact single muscle fibers</title><source>PubMed</source><creator>Pézolet, M. ; Pigeon-Gosselin, M. ; Nadeau, J. ; Caillé, J.P.</creator><creatorcontrib>Pézolet, M. ; Pigeon-Gosselin, M. ; Nadeau, J. ; Caillé, J.P.</creatorcontrib><description>The 500 to 1,800-cm-1 region of the Raman spectra of intact single muscle fibers from the giant barnacle are dominated by bands caused by the protein component of the fibers. The frequency and the intensity of the conformationally sensitive bands indicate that the contractile proteins adopt a predominantly alpha-helical structure and are not affected when the contractile state of the fibers is changed from relaxed to contracted by addition of ATP and Ca. However, the contraction induces a decrease of the scattering intensity of some of the Raman bands caused by the acidic and tryptophan side chains, showing that these amino acids are involved during the generation of tension.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(80)85036-3</identifier><identifier>PMID: 7272428</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphate - pharmacology ; Animals ; Biophysical Phenomena ; Biophysics ; Calcium - pharmacology ; Contractile Proteins - physiology ; Lasers ; Magnesium - pharmacology ; Muscle Contraction - drug effects ; Muscle Proteins - physiology ; Muscles - physiology ; Protein Conformation ; Space life sciences ; Spectrum Analysis, Raman - instrumentation ; Thoracica - physiology</subject><ispartof>Biophysical journal, 1980-07, Vol.31 (1), p.1-8</ispartof><rights>1980 The Biophysical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-ba2812f8f9dbf4db0bd8b2508dafe52141cbc8b57c64f887423a92977db722a53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1328760/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1328760/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7272428$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pézolet, M.</creatorcontrib><creatorcontrib>Pigeon-Gosselin, M.</creatorcontrib><creatorcontrib>Nadeau, J.</creatorcontrib><creatorcontrib>Caillé, J.P.</creatorcontrib><title>Laser Raman scattering. A molecular probe of the contractile state of intact single muscle fibers</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The 500 to 1,800-cm-1 region of the Raman spectra of intact single muscle fibers from the giant barnacle are dominated by bands caused by the protein component of the fibers. The frequency and the intensity of the conformationally sensitive bands indicate that the contractile proteins adopt a predominantly alpha-helical structure and are not affected when the contractile state of the fibers is changed from relaxed to contracted by addition of ATP and Ca. However, the contraction induces a decrease of the scattering intensity of some of the Raman bands caused by the acidic and tryptophan side chains, showing that these amino acids are involved during the generation of tension.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Animals</subject><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>Calcium - pharmacology</subject><subject>Contractile Proteins - physiology</subject><subject>Lasers</subject><subject>Magnesium - pharmacology</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle Proteins - physiology</subject><subject>Muscles - physiology</subject><subject>Protein Conformation</subject><subject>Space life sciences</subject><subject>Spectrum Analysis, Raman - instrumentation</subject><subject>Thoracica - physiology</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1980</creationdate><recordtype>article</recordtype><recordid>eNqFUctqHDEQFCHG2Tj5BINOITmMLWmkkfZiY0wehgWDnZyFpGnZCjOjtaQx5O-tfbDEJ5-a7qrqLroQOqXkjBLand8TQrqm5UvxVZFvSpC2du_QggrOGkJU9x4tDpQP6GPOfwmhTBB6jI4lk4wztUBmZTIkfGdGM-HsTCmQwvRwhq_wGAdw82ASXqdoAUePyyNgF6eSjCthAJyLKVsgTKWOcK7SOh7n7GrxwULKn9CRN0OGz_t6gv78-P77-lezuv15c321apxoSWmsYYoyr_yyt573lthe2epW9caDYJRTZ52yQrqOe6UkZ61ZsqWUvZWMGdGeoIvd3vVsR-gdbGwOep3CaNI_HU3Qr5EpPOqH-Kxpy5TsSF3wZb8gxacZctFjyA6GwUwQ56ylEJx2jFei2BFdijkn8IcjlOhNNnqbjd48Xiuit9notupO_3d4UO3DqPjlDof6pucASWcXYHLQhwSu6D6GNy68AILaoII</recordid><startdate>19800701</startdate><enddate>19800701</enddate><creator>Pézolet, M.</creator><creator>Pigeon-Gosselin, M.</creator><creator>Nadeau, J.</creator><creator>Caillé, J.P.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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><scope>5PM</scope></search><sort><creationdate>19800701</creationdate><title>Laser Raman scattering. A molecular probe of the contractile state of intact single muscle fibers</title><author>Pézolet, M. ; Pigeon-Gosselin, M. ; Nadeau, J. ; Caillé, J.P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-ba2812f8f9dbf4db0bd8b2508dafe52141cbc8b57c64f887423a92977db722a53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1980</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Animals</topic><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>Calcium - pharmacology</topic><topic>Contractile Proteins - physiology</topic><topic>Lasers</topic><topic>Magnesium - pharmacology</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle Proteins - physiology</topic><topic>Muscles - physiology</topic><topic>Protein Conformation</topic><topic>Space life sciences</topic><topic>Spectrum Analysis, Raman - instrumentation</topic><topic>Thoracica - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pézolet, M.</creatorcontrib><creatorcontrib>Pigeon-Gosselin, M.</creatorcontrib><creatorcontrib>Nadeau, J.</creatorcontrib><creatorcontrib>Caillé, J.P.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pézolet, M.</au><au>Pigeon-Gosselin, M.</au><au>Nadeau, J.</au><au>Caillé, J.P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Laser Raman scattering. A molecular probe of the contractile state of intact single muscle fibers</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1980-07-01</date><risdate>1980</risdate><volume>31</volume><issue>1</issue><spage>1</spage><epage>8</epage><pages>1-8</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The 500 to 1,800-cm-1 region of the Raman spectra of intact single muscle fibers from the giant barnacle are dominated by bands caused by the protein component of the fibers. The frequency and the intensity of the conformationally sensitive bands indicate that the contractile proteins adopt a predominantly alpha-helical structure and are not affected when the contractile state of the fibers is changed from relaxed to contracted by addition of ATP and Ca. However, the contraction induces a decrease of the scattering intensity of some of the Raman bands caused by the acidic and tryptophan side chains, showing that these amino acids are involved during the generation of tension.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7272428</pmid><doi>10.1016/S0006-3495(80)85036-3</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-3495 |
ispartof | Biophysical journal, 1980-07, Vol.31 (1), p.1-8 |
issn | 0006-3495 1542-0086 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1328760 |
source | PubMed |
subjects | Adenosine Triphosphate - pharmacology Animals Biophysical Phenomena Biophysics Calcium - pharmacology Contractile Proteins - physiology Lasers Magnesium - pharmacology Muscle Contraction - drug effects Muscle Proteins - physiology Muscles - physiology Protein Conformation Space life sciences Spectrum Analysis, Raman - instrumentation Thoracica - physiology |
title | Laser Raman scattering. A molecular probe of the contractile state of intact single muscle fibers |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T02%3A15%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Laser%20Raman%20scattering.%20A%20molecular%20probe%20of%20the%20contractile%20state%20of%20intact%20single%20muscle%20fibers&rft.jtitle=Biophysical%20journal&rft.au=P%C3%A9zolet,%20M.&rft.date=1980-07-01&rft.volume=31&rft.issue=1&rft.spage=1&rft.epage=8&rft.pages=1-8&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1016/S0006-3495(80)85036-3&rft_dat=%3Cproquest_pubme%3E75541624%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c530t-ba2812f8f9dbf4db0bd8b2508dafe52141cbc8b57c64f887423a92977db722a53%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=75541624&rft_id=info:pmid/7272428&rfr_iscdi=true |