A Method for Probing the Topography and Interactions of Proteins: Footprinting of Myoglobin
We describe a procedure for mapping residues on the surface of a protein molecule to its sequence, using a scheme that is analogous to nucleic acid footprinting. The protein is end labeled radioactively and subjected to limited proteolysis, and the products are analyzed by denaturing polyacrylamide...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1995-03, Vol.92 (6), p.2111-2115 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 92 |
| creator | Zhong, Min Lin, Laura Kallenbach, Neville R. |
| description | We describe a procedure for mapping residues on the surface of a protein molecule to its sequence, using a scheme that is analogous to nucleic acid footprinting. The protein is end labeled radioactively and subjected to limited proteolysis, and the products are analyzed by denaturing polyacrylamide gel electrophoresis and autoradiography. The method is tested with the heme protein myoglobin and applied to mapping the (unknown) surface of the molecule lacking the heme group: apomyoglobin. Sites of protein-protein interaction can be identified, as illustrated by footprinting the association between myoglobin and an anti-myoglobin monoclonal antibody. |
| doi_str_mv | 10.1073/pnas.92.6.2111 |
| format | Article |
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The protein is end labeled radioactively and subjected to limited proteolysis, and the products are analyzed by denaturing polyacrylamide gel electrophoresis and autoradiography. The method is tested with the heme protein myoglobin and applied to mapping the (unknown) surface of the molecule lacking the heme group: apomyoglobin. 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The protein is end labeled radioactively and subjected to limited proteolysis, and the products are analyzed by denaturing polyacrylamide gel electrophoresis and autoradiography. The method is tested with the heme protein myoglobin and applied to mapping the (unknown) surface of the molecule lacking the heme group: apomyoglobin. Sites of protein-protein interaction can be identified, as illustrated by footprinting the association between myoglobin and an anti-myoglobin monoclonal antibody.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Monoclonal</subject><subject>Apoproteins - chemistry</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Cattle</subject><subject>Cloning, Molecular</subject><subject>Endopeptidases</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Gels</subject><subject>Isotope Labeling - methods</subject><subject>Marine</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Monoclonal antibodies</subject><subject>Myocardium - metabolism</subject><subject>Myoglobin - biosynthesis</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobin - metabolism</subject><subject>Nucleic acids</subject><subject>Phosphorus Radioisotopes</subject><subject>Physeter</subject><subject>Product labeling</subject><subject>Protein Kinases - chemistry</subject><subject>Protein Kinases - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Reactivity</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Spermatozoa</subject><subject>Whales</subject><subject>Whales & whaling</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EKkvhygkki0NvCf6I7QRxqaoWKrWCQzlxsBzH3s0qawfbqbr_fR3tslo4tKc5vN97mpkHwHuMSowE_Tw6FcuGlLwkGOMXYIFRgwteNeglWCBERFFXpHoN3sS4Rgg1rEYn4ETUDSGULsDvc3hr0sp30PoAfwbf9m4J08rAOz_6ZVDjaguV6-C1SyYonXrvIvR2RpPpXfwCr7xPY-hdmp1Zud365TDnvAWvrBqiebefp-DX1eXdxffi5se364vzm0IzzFIhUMsFY00nKFHUCoY60zJT1UQbggTjjFBc6dZYwhEmnFlmraq10bbK59T0FHzd5Y5TuzGdNi4FNci800aFrfSql_8qrl_Jpb-X-TGUZvvZ3h78n8nEJDd91GYYlDN-ilIIXGOKngcxF7hiDGXw03_g2k_B5R9IgnIU53xOK3eQDj7GYOxhYYzkXK2cq5UNkVzO1WbDx-MzD_i-yyN99v1Vj_1nT-nSTsOQzEPK4IcduI7JhwNJKOdNRegjyMjA1A</recordid><startdate>19950314</startdate><enddate>19950314</enddate><creator>Zhong, Min</creator><creator>Lin, Laura</creator><creator>Kallenbach, Neville R.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>F1W</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19950314</creationdate><title>A Method for Probing the Topography and Interactions of Proteins: Footprinting of Myoglobin</title><author>Zhong, Min ; Lin, Laura ; Kallenbach, Neville R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c515t-70b67559d732a3f750deb5e482ce2075652314cbef2601265f5ffa8cecf495883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Monoclonal</topic><topic>Apoproteins - chemistry</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Cattle</topic><topic>Cloning, Molecular</topic><topic>Endopeptidases</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Gels</topic><topic>Isotope Labeling - methods</topic><topic>Marine</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Monoclonal antibodies</topic><topic>Myocardium - metabolism</topic><topic>Myoglobin - biosynthesis</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobin - metabolism</topic><topic>Nucleic acids</topic><topic>Phosphorus Radioisotopes</topic><topic>Physeter</topic><topic>Product labeling</topic><topic>Protein Kinases - chemistry</topic><topic>Protein Kinases - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Reactivity</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Spermatozoa</topic><topic>Whales</topic><topic>Whales & whaling</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhong, Min</creatorcontrib><creatorcontrib>Lin, Laura</creatorcontrib><creatorcontrib>Kallenbach, Neville R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhong, Min</au><au>Lin, Laura</au><au>Kallenbach, Neville R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Method for Probing the Topography and Interactions of Proteins: Footprinting of Myoglobin</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1995-03-14</date><risdate>1995</risdate><volume>92</volume><issue>6</issue><spage>2111</spage><epage>2115</epage><pages>2111-2115</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>We describe a procedure for mapping residues on the surface of a protein molecule to its sequence, using a scheme that is analogous to nucleic acid footprinting. 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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1995-03, Vol.92 (6), p.2111-2115 |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Adenosine Triphosphate - metabolism Amino Acid Sequence Animals Antibodies Antibodies, Monoclonal Apoproteins - chemistry Binding Sites Biochemistry Cattle Cloning, Molecular Endopeptidases Enzymes Escherichia coli Gels Isotope Labeling - methods Marine Models, Molecular Molecular Sequence Data Monoclonal antibodies Myocardium - metabolism Myoglobin - biosynthesis Myoglobin - chemistry Myoglobin - metabolism Nucleic acids Phosphorus Radioisotopes Physeter Product labeling Protein Kinases - chemistry Protein Kinases - metabolism Protein Structure, Secondary Proteins Proteins - chemistry Reactivity Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - metabolism Spermatozoa Whales Whales & whaling |
| title | A Method for Probing the Topography and Interactions of Proteins: Footprinting of Myoglobin |
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