Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study
The solution structure of human insulin-like growth factor 1 has been investigated with a combination of nuclear magnetic resonance and restrained molecular dynamics methods. The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologo...
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| Veröffentlicht in: | Biochemistry (Easton) 1991-06, Vol.30 (22), p.5484-5491 |
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| container_title | Biochemistry (Easton) |
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| creator | Cooke, Robert M Harvey, Timothy S Campbell, Iain D |
| description | The solution structure of human insulin-like growth factor 1 has been investigated with a combination of nuclear magnetic resonance and restrained molecular dynamics methods. The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologous to insulin are well-defined, while the remainder of the molecule exhibits greater disorder. The resultant structures have been used to visualize the sites for interaction with a number of physiologically important proteins. |
| doi_str_mv | 10.1021/bi00236a022 |
| format | Article |
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The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologous to insulin are well-defined, while the remainder of the molecule exhibits greater disorder. The resultant structures have been used to visualize the sites for interaction with a number of physiologically important proteins.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00236a022</identifier><identifier>PMID: 2036417</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>550601 - Medicine- Unsealed Radionuclides in Diagnostics ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; ANIMALS ; AQUEOUS SOLUTIONS ; Binding Sites ; Biological and medical sciences ; CHEMICAL SHIFT ; DISPERSIONS ; Fundamental and applied biological sciences. Psychology ; GROWTH FACTORS ; HEAVY WATER ; HORMONES ; Humans ; HYDROGEN COMPOUNDS ; INSULIN ; Insulin - chemistry ; Insulin-Like Growth Factor I - chemistry ; MAGNETIC RESONANCE ; Magnetic Resonance Spectroscopy ; MAMMALS ; MAN ; MITOGENS ; MIXTURES ; Molecular Sequence Data ; NUCLEAR MAGNETIC RESONANCE ; ORGANIC COMPOUNDS ; OVERHAUSER EFFECT ; OXYGEN COMPOUNDS ; PEPTIDE HORMONES ; PRIMATES ; Protein Conformation ; Protein hormones. Growth factors. 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The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologous to insulin are well-defined, while the remainder of the molecule exhibits greater disorder. The resultant structures have been used to visualize the sites for interaction with a number of physiologically important proteins.</description><subject>550601 - Medicine- Unsealed Radionuclides in Diagnostics</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ANIMALS</subject><subject>AQUEOUS SOLUTIONS</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>CHEMICAL SHIFT</subject><subject>DISPERSIONS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GROWTH FACTORS</subject><subject>HEAVY WATER</subject><subject>HORMONES</subject><subject>Humans</subject><subject>HYDROGEN COMPOUNDS</subject><subject>INSULIN</subject><subject>Insulin - chemistry</subject><subject>Insulin-Like Growth Factor I - chemistry</subject><subject>MAGNETIC RESONANCE</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>MAMMALS</subject><subject>MAN</subject><subject>MITOGENS</subject><subject>MIXTURES</subject><subject>Molecular Sequence Data</subject><subject>NUCLEAR MAGNETIC RESONANCE</subject><subject>ORGANIC COMPOUNDS</subject><subject>OVERHAUSER EFFECT</subject><subject>OXYGEN COMPOUNDS</subject><subject>PEPTIDE HORMONES</subject><subject>PRIMATES</subject><subject>Protein Conformation</subject><subject>Protein hormones. Growth factors. Cytokines</subject><subject>PROTEINS</subject><subject>RADIOLOGY AND NUCLEAR MEDICINE</subject><subject>RESONANCE</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>SOLUTIONS</subject><subject>Structure-Activity Relationship</subject><subject>VERTEBRATES</subject><subject>WATER</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0cuLFDEQB-BGlHVcPXkWgqAepLWSfiTxJosvHHBhRvAWMnnsZLc7WfNA5-LfbpYeVg-Cp1DUR6WoX9M8xvAKA8Gvdw6AdKMEQu40KzwQaHvOh7vNCgDGlvAR7jcPUrqsZQ-0P2lOCHRjj-mq-bUJU8kueJRyLCqXaFCwaF9m6ZHzqUzOt5O7Mugihh95j6xUOUSE3yCJfFGTkRHN8sKb7BSKJgUvvTJIen1T5SidNxrNYTKqTNXqg5ezU6n-V_ThYXPPyimZR8f3tPn6_t327GO7_vLh09nbdSt70uWWE8k4tth21jLaEwpMc0U1dJzCMDKgBveGM20JpkoTZQETzuhgNNsxqbvT5ukyN6TsRFIuG7VXwXujshiA0nHsK3q-oOsYvpe6vJhdUmaapDehJMFgYJgN7L8Qj_XSBHCFLxeoYkgpGiuuo5tlPAgM4iY78Vd2VT85ji272ehbewyr9p8d-zIpOdlYL-3Sn5Gc1g3pWF27OJey-Xnbl_FKjLSjg9iebwTBa3y-_fZZbKp_sXipkrgMJfoaxT83_A2-Xr0p</recordid><startdate>19910601</startdate><enddate>19910601</enddate><creator>Cooke, Robert M</creator><creator>Harvey, Timothy S</creator><creator>Campbell, Iain D</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>19910601</creationdate><title>Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study</title><author>Cooke, Robert M ; Harvey, Timothy S ; Campbell, Iain D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a423t-92a891f1f3ff8742708d9c7d0397056807e14e98df217cd2cf0129875ed8b8ad3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>550601 - Medicine- Unsealed Radionuclides in Diagnostics</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>ANIMALS</topic><topic>AQUEOUS SOLUTIONS</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>CHEMICAL SHIFT</topic><topic>DISPERSIONS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GROWTH FACTORS</topic><topic>HEAVY WATER</topic><topic>HORMONES</topic><topic>Humans</topic><topic>HYDROGEN COMPOUNDS</topic><topic>INSULIN</topic><topic>Insulin - chemistry</topic><topic>Insulin-Like Growth Factor I - chemistry</topic><topic>MAGNETIC RESONANCE</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>MAMMALS</topic><topic>MAN</topic><topic>MITOGENS</topic><topic>MIXTURES</topic><topic>Molecular Sequence Data</topic><topic>NUCLEAR MAGNETIC RESONANCE</topic><topic>ORGANIC COMPOUNDS</topic><topic>OVERHAUSER EFFECT</topic><topic>OXYGEN COMPOUNDS</topic><topic>PEPTIDE HORMONES</topic><topic>PRIMATES</topic><topic>Protein Conformation</topic><topic>Protein hormones. Growth factors. Cytokines</topic><topic>PROTEINS</topic><topic>RADIOLOGY AND NUCLEAR MEDICINE</topic><topic>RESONANCE</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>SOLUTIONS</topic><topic>Structure-Activity Relationship</topic><topic>VERTEBRATES</topic><topic>WATER</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cooke, Robert M</creatorcontrib><creatorcontrib>Harvey, Timothy S</creatorcontrib><creatorcontrib>Campbell, Iain D</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>OSTI.GOV</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cooke, Robert M</au><au>Harvey, Timothy S</au><au>Campbell, Iain D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>1991-06-01</date><risdate>1991</risdate><volume>30</volume><issue>22</issue><spage>5484</spage><epage>5491</epage><pages>5484-5491</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>The solution structure of human insulin-like growth factor 1 has been investigated with a combination of nuclear magnetic resonance and restrained molecular dynamics methods. The results show that the solution structure is similar to that of insulin, but minor differences exist. The regions homologous to insulin are well-defined, while the remainder of the molecule exhibits greater disorder. The resultant structures have been used to visualize the sites for interaction with a number of physiologically important proteins.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>2036417</pmid><doi>10.1021/bi00236a022</doi><tpages>8</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1991-06, Vol.30 (22), p.5484-5491 |
| issn | 0006-2960 1520-4995 |
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| source | MEDLINE; American Chemical Society Journals |
| subjects | 550601 - Medicine- Unsealed Radionuclides in Diagnostics Amino Acid Sequence Analytical, structural and metabolic biochemistry ANIMALS AQUEOUS SOLUTIONS Binding Sites Biological and medical sciences CHEMICAL SHIFT DISPERSIONS Fundamental and applied biological sciences. Psychology GROWTH FACTORS HEAVY WATER HORMONES Humans HYDROGEN COMPOUNDS INSULIN Insulin - chemistry Insulin-Like Growth Factor I - chemistry MAGNETIC RESONANCE Magnetic Resonance Spectroscopy MAMMALS MAN MITOGENS MIXTURES Molecular Sequence Data NUCLEAR MAGNETIC RESONANCE ORGANIC COMPOUNDS OVERHAUSER EFFECT OXYGEN COMPOUNDS PEPTIDE HORMONES PRIMATES Protein Conformation Protein hormones. Growth factors. Cytokines PROTEINS RADIOLOGY AND NUCLEAR MEDICINE RESONANCE Sequence Homology, Nucleic Acid SOLUTIONS Structure-Activity Relationship VERTEBRATES WATER |
| title | Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study |
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