Identification and secondary structure analysis of a keratin-like fibrous protein discovered in ligament of the bivalve Siliqua radiata
A novel keratin-like fibrous protein K58 with molecular weight of about 58 kDa was discovered in bivalve Siliqua radiata ligament and identified by amino acid composition and MALDI-TOF-TOF analysis. We found that the protein is composed of cylindrical fibers (∼160 nm in diameter) and contains high g...
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| Veröffentlicht in: | Biochemistry (Moscow) 2011-11, Vol.76 (11), p.1227-1232 |
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| creator | Huang, Zengqiong Zhang, Gangsheng |
| description | A novel keratin-like fibrous protein K58 with molecular weight of about 58 kDa was discovered in bivalve
Siliqua radiata
ligament and identified by amino acid composition and MALDI-TOF-TOF analysis. We found that the protein is composed of cylindrical fibers (∼160 nm in diameter) and contains high glycine (27.4%) and phenylalanine (10.5%) contents. Furthermore, it is homologous to keratin type II cytoskeletal 1, with repeat motifs of SGGG and SYGSGG. FTIR and secondary structure analysis indicate that K58 is composed of 46.2% β-sheet, 33.4% β-turn, 13.1% α-helix, and 4.7% disordered structure. This structure feature is closely related to the superior tensile strength, elasticity, and solvent resistance property of K58. These discoveries provide some evidence for evolution of keratin and fibrous proteins and prompt further studies of ligament fibrous proteins. |
| doi_str_mv | 10.1134/S0006297911110046 |
| format | Article |
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Siliqua radiata
ligament and identified by amino acid composition and MALDI-TOF-TOF analysis. We found that the protein is composed of cylindrical fibers (∼160 nm in diameter) and contains high glycine (27.4%) and phenylalanine (10.5%) contents. Furthermore, it is homologous to keratin type II cytoskeletal 1, with repeat motifs of SGGG and SYGSGG. FTIR and secondary structure analysis indicate that K58 is composed of 46.2% β-sheet, 33.4% β-turn, 13.1% α-helix, and 4.7% disordered structure. This structure feature is closely related to the superior tensile strength, elasticity, and solvent resistance property of K58. These discoveries provide some evidence for evolution of keratin and fibrous proteins and prompt further studies of ligament fibrous proteins.</description><identifier>ISSN: 0006-2979</identifier><identifier>EISSN: 1608-3040</identifier><identifier>DOI: 10.1134/S0006297911110046</identifier><identifier>PMID: 22117549</identifier><language>eng</language><publisher>Dordrecht: SP MAIK Nauka/Interperiodica</publisher><subject>Amino acids ; Animals ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Bioorganic Chemistry ; Bivalvia - chemistry ; Fibers ; Glycine ; Glycine - analysis ; Humans ; Keratin ; Keratins - chemistry ; Life Sciences ; Ligaments ; Ligaments - chemistry ; Microbiology ; Mollusks ; Phenylalanine ; Phenylalanine - analysis ; Protein Structure, Secondary ; Proteins ; Scleroproteins - chemistry ; Scleroproteins - ultrastructure ; Sequence Homology, Amino Acid ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><ispartof>Biochemistry (Moscow), 2011-11, Vol.76 (11), p.1227-1232</ispartof><rights>Pleiades Publishing, Ltd. 2011</rights><rights>COPYRIGHT 2011 Springer</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-e5cb1c0951f0a37e00dec3068d4e8aaf5df78e1719ecf39dd9ba5843141493b03</citedby><cites>FETCH-LOGICAL-c437t-e5cb1c0951f0a37e00dec3068d4e8aaf5df78e1719ecf39dd9ba5843141493b03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1134/S0006297911110046$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1134/S0006297911110046$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22117549$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, Zengqiong</creatorcontrib><creatorcontrib>Zhang, Gangsheng</creatorcontrib><title>Identification and secondary structure analysis of a keratin-like fibrous protein discovered in ligament of the bivalve Siliqua radiata</title><title>Biochemistry (Moscow)</title><addtitle>Biochemistry Moscow</addtitle><addtitle>Biochemistry (Mosc)</addtitle><description>A novel keratin-like fibrous protein K58 with molecular weight of about 58 kDa was discovered in bivalve
Siliqua radiata
ligament and identified by amino acid composition and MALDI-TOF-TOF analysis. We found that the protein is composed of cylindrical fibers (∼160 nm in diameter) and contains high glycine (27.4%) and phenylalanine (10.5%) contents. Furthermore, it is homologous to keratin type II cytoskeletal 1, with repeat motifs of SGGG and SYGSGG. FTIR and secondary structure analysis indicate that K58 is composed of 46.2% β-sheet, 33.4% β-turn, 13.1% α-helix, and 4.7% disordered structure. This structure feature is closely related to the superior tensile strength, elasticity, and solvent resistance property of K58. These discoveries provide some evidence for evolution of keratin and fibrous proteins and prompt further studies of ligament fibrous proteins.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Bioorganic Chemistry</subject><subject>Bivalvia - chemistry</subject><subject>Fibers</subject><subject>Glycine</subject><subject>Glycine - analysis</subject><subject>Humans</subject><subject>Keratin</subject><subject>Keratins - chemistry</subject><subject>Life Sciences</subject><subject>Ligaments</subject><subject>Ligaments - chemistry</subject><subject>Microbiology</subject><subject>Mollusks</subject><subject>Phenylalanine</subject><subject>Phenylalanine - analysis</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Scleroproteins - chemistry</subject><subject>Scleroproteins - ultrastructure</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><issn>0006-2979</issn><issn>1608-3040</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kcluFDEQhi0EIkPgAbggCw6cOpTb7sXHKGKJFCmHwLlVbZcHJ70ktnukPEFeG7cmgEiCfbCq6vvLtTD2VsCREFJ9ugCAutSNFvkAqPoZ24ga2kKCgudss4aLNX7AXsV4mc0StHzJDspSiKZSesPuTi1NyTtvMPl54jhZHsnMk8Vwy2MKi0lLoOzH4Tb6yGfHkV9RyPhUDP6KuPN9mJfIr8OcyE_c-mjmHQWyPFuD3-KYv1iF6Sfx3u9w2BG_8IO_WZAHtB4TvmYvHA6R3ty_h-zHl8_fT74VZ-dfT0-OzwqjZJMKqkwvDOhKOEDZEIAlI6FuraIW0VXWNS2JRmgyTmprdY9Vq6RQQmnZgzxkH_d5c7U3C8XUjblcGgacKDfRaairSjdqJd8_IC_nJeQxrJDSIFWtM_RhD21xoM5Pbk4BzZqyO5aqqrVqmzXV0RNUvpZGn2dNzmf_PwKxF5gwxxjIddfBj3kjnYBuXX33aPVZ8-6-3qUfyf5R_N51Bso9EHNo2lL429D_s_4CmO64qQ</recordid><startdate>20111101</startdate><enddate>20111101</enddate><creator>Huang, Zengqiong</creator><creator>Zhang, Gangsheng</creator><general>SP MAIK Nauka/Interperiodica</general><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20111101</creationdate><title>Identification and secondary structure analysis of a keratin-like fibrous protein discovered in ligament of the bivalve Siliqua radiata</title><author>Huang, Zengqiong ; Zhang, Gangsheng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-e5cb1c0951f0a37e00dec3068d4e8aaf5df78e1719ecf39dd9ba5843141493b03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Bioorganic Chemistry</topic><topic>Bivalvia - chemistry</topic><topic>Fibers</topic><topic>Glycine</topic><topic>Glycine - analysis</topic><topic>Humans</topic><topic>Keratin</topic><topic>Keratins - chemistry</topic><topic>Life Sciences</topic><topic>Ligaments</topic><topic>Ligaments - chemistry</topic><topic>Microbiology</topic><topic>Mollusks</topic><topic>Phenylalanine</topic><topic>Phenylalanine - analysis</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Scleroproteins - chemistry</topic><topic>Scleroproteins - ultrastructure</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, Zengqiong</creatorcontrib><creatorcontrib>Zhang, Gangsheng</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Moscow)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Zengqiong</au><au>Zhang, Gangsheng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and secondary structure analysis of a keratin-like fibrous protein discovered in ligament of the bivalve Siliqua radiata</atitle><jtitle>Biochemistry (Moscow)</jtitle><stitle>Biochemistry Moscow</stitle><addtitle>Biochemistry (Mosc)</addtitle><date>2011-11-01</date><risdate>2011</risdate><volume>76</volume><issue>11</issue><spage>1227</spage><epage>1232</epage><pages>1227-1232</pages><issn>0006-2979</issn><eissn>1608-3040</eissn><abstract>A novel keratin-like fibrous protein K58 with molecular weight of about 58 kDa was discovered in bivalve
Siliqua radiata
ligament and identified by amino acid composition and MALDI-TOF-TOF analysis. We found that the protein is composed of cylindrical fibers (∼160 nm in diameter) and contains high glycine (27.4%) and phenylalanine (10.5%) contents. Furthermore, it is homologous to keratin type II cytoskeletal 1, with repeat motifs of SGGG and SYGSGG. FTIR and secondary structure analysis indicate that K58 is composed of 46.2% β-sheet, 33.4% β-turn, 13.1% α-helix, and 4.7% disordered structure. This structure feature is closely related to the superior tensile strength, elasticity, and solvent resistance property of K58. These discoveries provide some evidence for evolution of keratin and fibrous proteins and prompt further studies of ligament fibrous proteins.</abstract><cop>Dordrecht</cop><pub>SP MAIK Nauka/Interperiodica</pub><pmid>22117549</pmid><doi>10.1134/S0006297911110046</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino acids Animals Biochemistry Biomedical and Life Sciences Biomedicine Bioorganic Chemistry Bivalvia - chemistry Fibers Glycine Glycine - analysis Humans Keratin Keratins - chemistry Life Sciences Ligaments Ligaments - chemistry Microbiology Mollusks Phenylalanine Phenylalanine - analysis Protein Structure, Secondary Proteins Scleroproteins - chemistry Scleroproteins - ultrastructure Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| title | Identification and secondary structure analysis of a keratin-like fibrous protein discovered in ligament of the bivalve Siliqua radiata |
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