Loading…
Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides
Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1–16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and...
Saved in:
Published in: | Biochemical and biophysical research communications 2007-12, Vol.364 (3), p.608-613 |
---|---|
Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites 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-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003 |
---|---|
cites | cdi_FETCH-LOGICAL-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003 |
container_end_page | 613 |
container_issue | 3 |
container_start_page | 608 |
container_title | Biochemical and biophysical research communications |
container_volume | 364 |
creator | Pal-Bhowmick, Ipsita Pati Pandey, Ramendra Jarori, Gotam K. Kar, Santosh Sahal, Dinkar |
description | Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1–16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and NMR analyses have revealed that the physicochemical and conformational properties of the S peptide are distinct from those of its retro and retro-inverso analogs. On the functional side, while the S peptide complemented the S protein to give RNase activity, was recognized by anti-S peptide antibodies and induced T cell proliferation, neither the retro nor the retro-inverso S peptides could do so. |
doi_str_mv | 10.1016/j.bbrc.2007.10.056 |
format | article |
fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_21033021</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X07022115</els_id><sourcerecordid>19468066</sourcerecordid><originalsourceid>FETCH-LOGICAL-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003</originalsourceid><addsrcrecordid>eNqFkV-L1DAUxYMo7uzqF_BBCoJPdry3adMWfFkWXYUFwVHQp5A_t5ihk4xJuuC3N90Z8E2fkhx-54R7D2MvELYIKN7ut1pHs20A-iJsoROP2AZhhLpBaB-zDQCIuhnx-wW7TGkPgNiK8Sm7wH4UvG-GDfuxy3ExeYlqrpS31bR4k13w5ZnyYh2lKvjqi9PBL2Ymlajavaki5Riq3YPj4V47f08xrdqRjtlZSs_Yk0nNiZ6fzyv27cP7rzcf67vPt59uru9q0yLPddegMADEVT8J1LbT0ONglAY-2q4VVnUNR913emgN77mw3aQH3bYoFAoAfsVenXJDyk4m4zKZnyZ4TybLsgjOocFCvT5Rxxh-LZSyPLhkaJ6Vp7AkKYZ2KB8N_wVxbMUAQhSwOYEmhpQiTfIY3UHF3xJBrv3IvVz7kWs_q1b6KaaX5_RFH8j-tZwLKcC7E0BlZfeO4joReUPWxXUgG9y_8v8AAemf2Q</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19468066</pqid></control><display><type>article</type><title>Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides</title><source>ScienceDirect Journals</source><creator>Pal-Bhowmick, Ipsita ; Pati Pandey, Ramendra ; Jarori, Gotam K. ; Kar, Santosh ; Sahal, Dinkar</creator><creatorcontrib>Pal-Bhowmick, Ipsita ; Pati Pandey, Ramendra ; Jarori, Gotam K. ; Kar, Santosh ; Sahal, Dinkar</creatorcontrib><description>Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1–16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and NMR analyses have revealed that the physicochemical and conformational properties of the S peptide are distinct from those of its retro and retro-inverso analogs. On the functional side, while the S peptide complemented the S protein to give RNase activity, was recognized by anti-S peptide antibodies and induced T cell proliferation, neither the retro nor the retro-inverso S peptides could do so.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.10.056</identifier><identifier>PMID: 17963728</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; Amino Acid Sequence ; ANTIBODIES ; ANTIGENS ; Binding Sites ; CELL PROLIFERATION ; CYTIDINE ; DICHROISM ; ENZYME IMMUNOASSAY ; HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY ; Mimetics ; NITRIC OXIDE ; NMR ; NUCLEAR MAGNETIC RESONANCE ; OVERHAUSER EFFECT ; Peptide Fragments - chemistry ; Peptide Fragments - immunology ; Peptide Fragments - ultrastructure ; PEPTIDES ; Protein Binding ; Retro/retro-inverso peptides ; Ribonuclease ; Ribonucleases - chemistry ; Ribonucleases - immunology ; Ribonucleases - ultrastructure ; RNA-ASE ; S peptide ; Structure-Activity Relationship ; T cells ; T-Lymphocytes - immunology</subject><ispartof>Biochemical and biophysical research communications, 2007-12, Vol.364 (3), p.608-613</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003</citedby><cites>FETCH-LOGICAL-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17963728$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/21033021$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Pal-Bhowmick, Ipsita</creatorcontrib><creatorcontrib>Pati Pandey, Ramendra</creatorcontrib><creatorcontrib>Jarori, Gotam K.</creatorcontrib><creatorcontrib>Kar, Santosh</creatorcontrib><creatorcontrib>Sahal, Dinkar</creatorcontrib><title>Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1–16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and NMR analyses have revealed that the physicochemical and conformational properties of the S peptide are distinct from those of its retro and retro-inverso analogs. On the functional side, while the S peptide complemented the S protein to give RNase activity, was recognized by anti-S peptide antibodies and induced T cell proliferation, neither the retro nor the retro-inverso S peptides could do so.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>Amino Acid Sequence</subject><subject>ANTIBODIES</subject><subject>ANTIGENS</subject><subject>Binding Sites</subject><subject>CELL PROLIFERATION</subject><subject>CYTIDINE</subject><subject>DICHROISM</subject><subject>ENZYME IMMUNOASSAY</subject><subject>HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY</subject><subject>Mimetics</subject><subject>NITRIC OXIDE</subject><subject>NMR</subject><subject>NUCLEAR MAGNETIC RESONANCE</subject><subject>OVERHAUSER EFFECT</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - immunology</subject><subject>Peptide Fragments - ultrastructure</subject><subject>PEPTIDES</subject><subject>Protein Binding</subject><subject>Retro/retro-inverso peptides</subject><subject>Ribonuclease</subject><subject>Ribonucleases - chemistry</subject><subject>Ribonucleases - immunology</subject><subject>Ribonucleases - ultrastructure</subject><subject>RNA-ASE</subject><subject>S peptide</subject><subject>Structure-Activity Relationship</subject><subject>T cells</subject><subject>T-Lymphocytes - immunology</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFkV-L1DAUxYMo7uzqF_BBCoJPdry3adMWfFkWXYUFwVHQp5A_t5ihk4xJuuC3N90Z8E2fkhx-54R7D2MvELYIKN7ut1pHs20A-iJsoROP2AZhhLpBaB-zDQCIuhnx-wW7TGkPgNiK8Sm7wH4UvG-GDfuxy3ExeYlqrpS31bR4k13w5ZnyYh2lKvjqi9PBL2Ymlajavaki5Riq3YPj4V47f08xrdqRjtlZSs_Yk0nNiZ6fzyv27cP7rzcf67vPt59uru9q0yLPddegMADEVT8J1LbT0ONglAY-2q4VVnUNR913emgN77mw3aQH3bYoFAoAfsVenXJDyk4m4zKZnyZ4TybLsgjOocFCvT5Rxxh-LZSyPLhkaJ6Vp7AkKYZ2KB8N_wVxbMUAQhSwOYEmhpQiTfIY3UHF3xJBrv3IvVz7kWs_q1b6KaaX5_RFH8j-tZwLKcC7E0BlZfeO4joReUPWxXUgG9y_8v8AAemf2Q</recordid><startdate>20071221</startdate><enddate>20071221</enddate><creator>Pal-Bhowmick, Ipsita</creator><creator>Pati Pandey, Ramendra</creator><creator>Jarori, Gotam K.</creator><creator>Kar, Santosh</creator><creator>Sahal, Dinkar</creator><general>Elsevier Inc</general><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>7T5</scope><scope>7TM</scope><scope>H94</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20071221</creationdate><title>Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides</title><author>Pal-Bhowmick, Ipsita ; Pati Pandey, Ramendra ; Jarori, Gotam K. ; Kar, Santosh ; Sahal, Dinkar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>Amino Acid Sequence</topic><topic>ANTIBODIES</topic><topic>ANTIGENS</topic><topic>Binding Sites</topic><topic>CELL PROLIFERATION</topic><topic>CYTIDINE</topic><topic>DICHROISM</topic><topic>ENZYME IMMUNOASSAY</topic><topic>HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY</topic><topic>Mimetics</topic><topic>NITRIC OXIDE</topic><topic>NMR</topic><topic>NUCLEAR MAGNETIC RESONANCE</topic><topic>OVERHAUSER EFFECT</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - immunology</topic><topic>Peptide Fragments - ultrastructure</topic><topic>PEPTIDES</topic><topic>Protein Binding</topic><topic>Retro/retro-inverso peptides</topic><topic>Ribonuclease</topic><topic>Ribonucleases - chemistry</topic><topic>Ribonucleases - immunology</topic><topic>Ribonucleases - ultrastructure</topic><topic>RNA-ASE</topic><topic>S peptide</topic><topic>Structure-Activity Relationship</topic><topic>T cells</topic><topic>T-Lymphocytes - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pal-Bhowmick, Ipsita</creatorcontrib><creatorcontrib>Pati Pandey, Ramendra</creatorcontrib><creatorcontrib>Jarori, Gotam K.</creatorcontrib><creatorcontrib>Kar, Santosh</creatorcontrib><creatorcontrib>Sahal, Dinkar</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pal-Bhowmick, Ipsita</au><au>Pati Pandey, Ramendra</au><au>Jarori, Gotam K.</au><au>Kar, Santosh</au><au>Sahal, Dinkar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-12-21</date><risdate>2007</risdate><volume>364</volume><issue>3</issue><spage>608</spage><epage>613</epage><pages>608-613</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Ribonuclease S peptide and S protein offer a unique complementation system to understand the finer features of molecular recognition. In the present study the S peptide (1–16), and its retro and retro-inverso analogs have been analyzed for their structural and biological attributes. RPHPLC, CD, and NMR analyses have revealed that the physicochemical and conformational properties of the S peptide are distinct from those of its retro and retro-inverso analogs. On the functional side, while the S peptide complemented the S protein to give RNase activity, was recognized by anti-S peptide antibodies and induced T cell proliferation, neither the retro nor the retro-inverso S peptides could do so.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17963728</pmid><doi>10.1016/j.bbrc.2007.10.056</doi><tpages>6</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0006-291X |
ispartof | Biochemical and biophysical research communications, 2007-12, Vol.364 (3), p.608-613 |
issn | 0006-291X 1090-2104 |
language | eng |
recordid | cdi_osti_scitechconnect_21033021 |
source | ScienceDirect Journals |
subjects | 60 APPLIED LIFE SCIENCES Amino Acid Sequence ANTIBODIES ANTIGENS Binding Sites CELL PROLIFERATION CYTIDINE DICHROISM ENZYME IMMUNOASSAY HIGH-PERFORMANCE LIQUID CHROMATOGRAPHY Mimetics NITRIC OXIDE NMR NUCLEAR MAGNETIC RESONANCE OVERHAUSER EFFECT Peptide Fragments - chemistry Peptide Fragments - immunology Peptide Fragments - ultrastructure PEPTIDES Protein Binding Retro/retro-inverso peptides Ribonuclease Ribonucleases - chemistry Ribonucleases - immunology Ribonucleases - ultrastructure RNA-ASE S peptide Structure-Activity Relationship T cells T-Lymphocytes - immunology |
title | Structural and functional studies on Ribonuclease S, retro S and retro-inverso S peptides |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T03%3A09%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20and%20functional%20studies%20on%20Ribonuclease%20S,%20retro%20S%20and%20retro-inverso%20S%20peptides&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Pal-Bhowmick,%20Ipsita&rft.date=2007-12-21&rft.volume=364&rft.issue=3&rft.spage=608&rft.epage=613&rft.pages=608-613&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2007.10.056&rft_dat=%3Cproquest_osti_%3E19468066%3C/proquest_osti_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c413t-5216c00e3a7f61bd5b0718cab039d546da5231b75b84c3736d5fb8b4416a16003%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=19468066&rft_id=info:pmid/17963728&rfr_iscdi=true |