Conformational properties of pairs of amino acids
Crystal structure data of 31 different globular proteins were analysed. Potentials for all 400 pairs of 20 amino acid residues in helix, extended structure, chain reversals and coil state were obtained. Analysis of these potentials showed that tripeptides of amino acid residues are not linear combin...
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| Veröffentlicht in: | International Journal of Peptide and Protein Research 1983-07, Vol.22 (1), p.83-91 |
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| container_title | International Journal of Peptide and Protein Research |
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| creator | KOLASKAR, A.S. RAMABRAHMAM, V. |
| description | Crystal structure data of 31 different globular proteins were analysed. Potentials for all 400 pairs of 20 amino acid residues in helix, extended structure, chain reversals and coil state were obtained. Analysis of these potentials showed that tripeptides of amino acid residues are not linear combinations of amino acids. The association effect of these tripeptides depends on the types of amino acids associated, the position of amino acids in the pair and the secondary structure in which the pair exists. This built‐in information in tripeptides should be used in polypeptide and protein folding studies. |
| doi_str_mv | 10.1111/j.1399-3011.1983.tb02072.x |
| format | Article |
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Potentials for all 400 pairs of 20 amino acid residues in helix, extended structure, chain reversals and coil state were obtained. Analysis of these potentials showed that tripeptides of amino acid residues are not linear combinations of amino acids. The association effect of these tripeptides depends on the types of amino acids associated, the position of amino acids in the pair and the secondary structure in which the pair exists. This built‐in information in tripeptides should be used in polypeptide and protein folding studies.</description><identifier>ISSN: 0367-8377</identifier><identifier>EISSN: 1399-3011</identifier><identifier>DOI: 10.1111/j.1399-3011.1983.tb02072.x</identifier><identifier>PMID: 6885252</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>amino acid pair potentials ; Amino Acids ; Crystallography ; data analysis ; globular proteins ; Hydrogen Bonding ; Protein Conformation ; protein crystal structures ; protein folding ; secondary structures ; Structure-Activity Relationship</subject><ispartof>International Journal of Peptide and Protein Research, 1983-07, Vol.22 (1), p.83-91</ispartof><rights>1983 Munksgaard International Publishers Ltd.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4383-987d65e39907f09cb836593e451a74802e2daf3df78c699ac57dc32ae8b9a9233</citedby><cites>FETCH-LOGICAL-c4383-987d65e39907f09cb836593e451a74802e2daf3df78c699ac57dc32ae8b9a9233</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1399-3011.1983.tb02072.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1399-3011.1983.tb02072.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6885252$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KOLASKAR, A.S.</creatorcontrib><creatorcontrib>RAMABRAHMAM, V.</creatorcontrib><title>Conformational properties of pairs of amino acids</title><title>International Journal of Peptide and Protein Research</title><addtitle>Int J Pept Protein Res</addtitle><description>Crystal structure data of 31 different globular proteins were analysed. Potentials for all 400 pairs of 20 amino acid residues in helix, extended structure, chain reversals and coil state were obtained. Analysis of these potentials showed that tripeptides of amino acid residues are not linear combinations of amino acids. The association effect of these tripeptides depends on the types of amino acids associated, the position of amino acids in the pair and the secondary structure in which the pair exists. This built‐in information in tripeptides should be used in polypeptide and protein folding studies.</description><subject>amino acid pair potentials</subject><subject>Amino Acids</subject><subject>Crystallography</subject><subject>data analysis</subject><subject>globular proteins</subject><subject>Hydrogen Bonding</subject><subject>Protein Conformation</subject><subject>protein crystal structures</subject><subject>protein folding</subject><subject>secondary structures</subject><subject>Structure-Activity Relationship</subject><issn>0367-8377</issn><issn>1399-3011</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkM1OwzAQhC0EKqXwCEgVB24JtjeObQ5IkEJBquBAgaPlJo7kkp9ip6J9exJS9YrYy640u7OjD6ELgkPS1tUyJCBlAJiQkEgBYbPAFHMabg7QcC8doiGGmAcCOD9GJ94vMYYIOB2gQSwEo4wOEUnqKq9dqRtbV7oYr1y9Mq6xxo_rfLzS1v0OurRVPdapzfwpOsp14c3Zro_Q28P9PHkMZi_Tp-R2FqQRCAik4FnMTBsG8xzLdCEgZhJMxIjmkcDU0EznkOVcpLGUOmU8S4FqIxZSSwowQpe9bxvpa218o0rrU1MUujL12iuBYyooif5cJBBD-6FzvO4XU1d770yuVs6W2m0VwaoDq5aqo6c6eqoDq3Zg1aY9Pt99WS9Kk-1PdyRb_abXv21htv9wVsndZCK6dEFvYH1jNnsD7T5VzIEz9fE8VQnM5oy9J-oVfgBHG5X2</recordid><startdate>198307</startdate><enddate>198307</enddate><creator>KOLASKAR, A.S.</creator><creator>RAMABRAHMAM, V.</creator><general>Blackwell Publishing Ltd</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>198307</creationdate><title>Conformational properties of pairs of amino acids</title><author>KOLASKAR, A.S. ; RAMABRAHMAM, V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4383-987d65e39907f09cb836593e451a74802e2daf3df78c699ac57dc32ae8b9a9233</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>amino acid pair potentials</topic><topic>Amino Acids</topic><topic>Crystallography</topic><topic>data analysis</topic><topic>globular proteins</topic><topic>Hydrogen Bonding</topic><topic>Protein Conformation</topic><topic>protein crystal structures</topic><topic>protein folding</topic><topic>secondary structures</topic><topic>Structure-Activity Relationship</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KOLASKAR, A.S.</creatorcontrib><creatorcontrib>RAMABRAHMAM, V.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>International Journal of Peptide and Protein Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KOLASKAR, A.S.</au><au>RAMABRAHMAM, V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Conformational properties of pairs of amino acids</atitle><jtitle>International Journal of Peptide and Protein Research</jtitle><addtitle>Int J Pept Protein Res</addtitle><date>1983-07</date><risdate>1983</risdate><volume>22</volume><issue>1</issue><spage>83</spage><epage>91</epage><pages>83-91</pages><issn>0367-8377</issn><eissn>1399-3011</eissn><abstract>Crystal structure data of 31 different globular proteins were analysed. 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| identifier | ISSN: 0367-8377 |
| ispartof | International Journal of Peptide and Protein Research, 1983-07, Vol.22 (1), p.83-91 |
| issn | 0367-8377 1399-3011 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80628214 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | amino acid pair potentials Amino Acids Crystallography data analysis globular proteins Hydrogen Bonding Protein Conformation protein crystal structures protein folding secondary structures Structure-Activity Relationship |
| title | Conformational properties of pairs of amino acids |
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