Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C14 Helix Formation

Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ) n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side...

Full description

Saved in:
Bibliographic Details
Published in:Organic letters 2013-09, Vol.15 (18), p.4866-4869
Main Authors: Basuroy, Krishnayan, Dinesh, Bhimareddy, Reddy, M. B. Madhusudana, Chandrappa, Siddapa, Raghothama, Srinivasarao, Shamala, Narayanaswamy, Balaram, Padmanabhan
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Crystallography, X-Ray
Models, Molecular
Molecular Structure
Peptides - chemical synthesis
Peptides - chemistry
Protein Conformation
Protein Structure, Secondary
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 4869
container_issue 18
container_start_page 4866
container_title Organic letters
container_volume 15
creator Basuroy, Krishnayan
Dinesh, Bhimareddy
Reddy, M. B. Madhusudana
Chandrappa, Siddapa
Raghothama, Srinivasarao
Shamala, Narayanaswamy
Balaram, Padmanabhan
description Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ) n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.
doi_str_mv 10.1021/ol402248s
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1449766859</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1449766859</sourcerecordid><originalsourceid>FETCH-LOGICAL-a156t-6bcc128a6b6af38d2da79c798c42c3c1f66629fba36e4d5fc6996d8dd170e3923</originalsourceid><addsrcrecordid>eNo9kNFKwzAYhYMobk4vfAHJjeBNNUnTtLmU4awwcKDDy5Am6ZbRNjNp0d35Cj6L7-FD-CRWNnf1H34-DocPgHOMrjEi-MZVFBFCs3AAhjghcZSihBzuM0MDcBLCCiHcf_gxGBCKEOIJGoKXeaNcE1ovbWM0zF3tXGUXrjbeKvj99fPxOTPr1moT4NPSvcHcLpZw5t3aNMG2G1g6D8eYwtxU9h1OnK9la11zCo5KWQVztrsjMJ_cPY_zaPp4_zC-nUYSJ6yNWKEUJplkBZNlnGmiZcpVyjNFiYoVLhljhJeFjJmhOikV45zpTGucIhNzEo_A1bZ37d1rZ0IrahuUqSrZGNcFgSnlKWNZwnv0Yod2RW20WHtbS78R_zJ64HILSBXEynW-6ZcLjMSfZLGXHP8ClkZt4A</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449766859</pqid></control><display><type>article</type><title>Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C14 Helix Formation</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read &amp; Publish Agreement 2022-2024 (Reading list)</source><creator>Basuroy, Krishnayan ; Dinesh, Bhimareddy ; Reddy, M. B. Madhusudana ; Chandrappa, Siddapa ; Raghothama, Srinivasarao ; Shamala, Narayanaswamy ; Balaram, Padmanabhan</creator><creatorcontrib>Basuroy, Krishnayan ; Dinesh, Bhimareddy ; Reddy, M. B. Madhusudana ; Chandrappa, Siddapa ; Raghothama, Srinivasarao ; Shamala, Narayanaswamy ; Balaram, Padmanabhan</creatorcontrib><description>Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ) n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.</description><identifier>ISSN: 1523-7060</identifier><identifier>EISSN: 1523-7052</identifier><identifier>DOI: 10.1021/ol402248s</identifier><identifier>PMID: 24000950</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Sequence ; Crystallography, X-Ray ; Models, Molecular ; Molecular Structure ; Peptides - chemical synthesis ; Peptides - chemistry ; Protein Conformation ; Protein Structure, Secondary</subject><ispartof>Organic letters, 2013-09, Vol.15 (18), p.4866-4869</ispartof><rights>Copyright © 2013 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24000950$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Basuroy, Krishnayan</creatorcontrib><creatorcontrib>Dinesh, Bhimareddy</creatorcontrib><creatorcontrib>Reddy, M. B. Madhusudana</creatorcontrib><creatorcontrib>Chandrappa, Siddapa</creatorcontrib><creatorcontrib>Raghothama, Srinivasarao</creatorcontrib><creatorcontrib>Shamala, Narayanaswamy</creatorcontrib><creatorcontrib>Balaram, Padmanabhan</creatorcontrib><title>Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C14 Helix Formation</title><title>Organic letters</title><addtitle>Org. Lett</addtitle><description>Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ) n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.</description><subject>Amino Acid Sequence</subject><subject>Crystallography, X-Ray</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Peptides - chemical synthesis</subject><subject>Peptides - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><issn>1523-7060</issn><issn>1523-7052</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNo9kNFKwzAYhYMobk4vfAHJjeBNNUnTtLmU4awwcKDDy5Am6ZbRNjNp0d35Cj6L7-FD-CRWNnf1H34-DocPgHOMrjEi-MZVFBFCs3AAhjghcZSihBzuM0MDcBLCCiHcf_gxGBCKEOIJGoKXeaNcE1ovbWM0zF3tXGUXrjbeKvj99fPxOTPr1moT4NPSvcHcLpZw5t3aNMG2G1g6D8eYwtxU9h1OnK9la11zCo5KWQVztrsjMJ_cPY_zaPp4_zC-nUYSJ6yNWKEUJplkBZNlnGmiZcpVyjNFiYoVLhljhJeFjJmhOikV45zpTGucIhNzEo_A1bZ37d1rZ0IrahuUqSrZGNcFgSnlKWNZwnv0Yod2RW20WHtbS78R_zJ64HILSBXEynW-6ZcLjMSfZLGXHP8ClkZt4A</recordid><startdate>20130920</startdate><enddate>20130920</enddate><creator>Basuroy, Krishnayan</creator><creator>Dinesh, Bhimareddy</creator><creator>Reddy, M. B. Madhusudana</creator><creator>Chandrappa, Siddapa</creator><creator>Raghothama, Srinivasarao</creator><creator>Shamala, Narayanaswamy</creator><creator>Balaram, Padmanabhan</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20130920</creationdate><title>Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C14 Helix Formation</title><author>Basuroy, Krishnayan ; Dinesh, Bhimareddy ; Reddy, M. B. Madhusudana ; Chandrappa, Siddapa ; Raghothama, Srinivasarao ; Shamala, Narayanaswamy ; Balaram, Padmanabhan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a156t-6bcc128a6b6af38d2da79c798c42c3c1f66629fba36e4d5fc6996d8dd170e3923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Amino Acid Sequence</topic><topic>Crystallography, X-Ray</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Peptides - chemical synthesis</topic><topic>Peptides - chemistry</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Basuroy, Krishnayan</creatorcontrib><creatorcontrib>Dinesh, Bhimareddy</creatorcontrib><creatorcontrib>Reddy, M. B. Madhusudana</creatorcontrib><creatorcontrib>Chandrappa, Siddapa</creatorcontrib><creatorcontrib>Raghothama, Srinivasarao</creatorcontrib><creatorcontrib>Shamala, Narayanaswamy</creatorcontrib><creatorcontrib>Balaram, Padmanabhan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Organic letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Basuroy, Krishnayan</au><au>Dinesh, Bhimareddy</au><au>Reddy, M. B. Madhusudana</au><au>Chandrappa, Siddapa</au><au>Raghothama, Srinivasarao</au><au>Shamala, Narayanaswamy</au><au>Balaram, Padmanabhan</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C14 Helix Formation</atitle><jtitle>Organic letters</jtitle><addtitle>Org. Lett</addtitle><date>2013-09-20</date><risdate>2013</risdate><volume>15</volume><issue>18</issue><spage>4866</spage><epage>4869</epage><pages>4866-4869</pages><issn>1523-7060</issn><eissn>1523-7052</eissn><abstract>Monosubstituted γ4-residues (γ4Leu, γ4Ile, and γ4Val) form helices even in short homooligomeric sequences. C14 helix formation is established by X-ray diffraction in homooligomeric (γ) n tetra-, hexa- and decapeptide sequences demonstrating the high propensity of γ residues, with proteinogenic side chains, to adopt locally folded conformations.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>24000950</pmid><doi>10.1021/ol402248s</doi><tpages>4</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1523-7060
ispartof Organic letters, 2013-09, Vol.15 (18), p.4866-4869
issn 1523-7060
1523-7052
language eng
recordid cdi_proquest_miscellaneous_1449766859
source American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects Amino Acid Sequence
Crystallography, X-Ray
Models, Molecular
Molecular Structure
Peptides - chemical synthesis
Peptides - chemistry
Protein Conformation
Protein Structure, Secondary
title Unconstrained Homooligomeric γ‑Peptides Show High Propensity for C14 Helix Formation
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-12T00%3A43%3A44IST&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=Unconstrained%20Homooligomeric%20%CE%B3%E2%80%91Peptides%20Show%20High%20Propensity%20for%20C14%20Helix%20Formation&rft.jtitle=Organic%20letters&rft.au=Basuroy,%20Krishnayan&rft.date=2013-09-20&rft.volume=15&rft.issue=18&rft.spage=4866&rft.epage=4869&rft.pages=4866-4869&rft.issn=1523-7060&rft.eissn=1523-7052&rft_id=info:doi/10.1021/ol402248s&rft_dat=%3Cproquest_pubme%3E1449766859%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a156t-6bcc128a6b6af38d2da79c798c42c3c1f66629fba36e4d5fc6996d8dd170e3923%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1449766859&rft_id=info:pmid/24000950&rfr_iscdi=true