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Natural abundance 15N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III
15N NMR assignments were made to the backbone amide nitrogen atoms at natural isotopic abundance of intact and reactive-site (Arg 5—Ile 6) hydrolyzed Cucurbita maxima trypsin inhibitor III (CMTI-III and CMTI-III*, respectively) by means of 2D proton-detected heteronuclear single bond chemical shift...
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| Published in: | FEBS letters 1992-06, Vol.304 (2), p.149-152 |
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| Language: | English |
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| container_end_page | 152 |
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| container_title | FEBS letters |
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| creator | Krishnamoorthi, Ramaswamy Nemmers, Sylvia Tobias, Brian |
| description | 15N NMR assignments were made to the backbone amide nitrogen atoms at natural isotopic abundance of intact and reactive-site (Arg
5—Ile
6) hydrolyzed
Cucurbita maxima trypsin inhibitor III (CMTI-III and CMTI-III*, respectively) by means of 2D proton-detected heteronuclear single bond chemical shift correlation (HSBC) spectroscopy, utilizing the previously made sequence-specific
1H NMR assignments (Krishnamoorthi et al. (1992) Biochemistry 31. 898–904). Comparison of the
15N chemical shifts of the two forms of the inhibitor molecule revealed significant changes not only for residues located near the reactive-site region, but also for those distantly located. Residues Cys
3, Arg
5, Leu
7, Met
8, Cys
10, Cys
16, Glu
19, His
25, Tyr
27, Cys
28 and Gly
28 showed significant chemical shift changes ranging from 0.3 to 6.1 ppm, thus indicating structural perturbations that were transmitted throughout the molecule. These findings confirm the earlier conclusions based on
1H NMR investigations. |
| doi_str_mv | 10.1016/0014-5793(92)80607-I |
| format | article |
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5—Ile
6) hydrolyzed
Cucurbita maxima trypsin inhibitor III (CMTI-III and CMTI-III*, respectively) by means of 2D proton-detected heteronuclear single bond chemical shift correlation (HSBC) spectroscopy, utilizing the previously made sequence-specific
1H NMR assignments (Krishnamoorthi et al. (1992) Biochemistry 31. 898–904). Comparison of the
15N chemical shifts of the two forms of the inhibitor molecule revealed significant changes not only for residues located near the reactive-site region, but also for those distantly located. Residues Cys
3, Arg
5, Leu
7, Met
8, Cys
10, Cys
16, Glu
19, His
25, Tyr
27, Cys
28 and Gly
28 showed significant chemical shift changes ranging from 0.3 to 6.1 ppm, thus indicating structural perturbations that were transmitted throughout the molecule. These findings confirm the earlier conclusions based on
1H NMR investigations.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(92)80607-I</identifier><identifier>PMID: 1618315</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>1H— 15N chemical shift correlation ; Activated Hageman factor ; Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Binding Sites ; Biological and medical sciences ; Blood coagulation ; CMTI ; Cucurbita maxima ; Cucurbita maxima trypsin inhibitor ; Disaccharides ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Glucans ; heteronuclear single bond chemical shift correlation spectroscopy ; high-performance liquid chromatography ; HPLC ; HSBC ; Hydrolases ; Hydrolysis ; Inhibitor ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; NMR ; nuclear magnetic resonance ; parts per million ; Peptide Fragments - chemistry ; Plant Proteins - chemistry ; Plants, Edible - chemistry ; ppm ; Pumpkin ; Serine protease ; Trypsin ; Trypsin Inhibitors - chemistry</subject><ispartof>FEBS letters, 1992-06, Vol.304 (2), p.149-152</ispartof><rights>1992</rights><rights>FEBS Letters 304 (1992) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/001457939280607I$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3540,27915,27916,45771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5319043$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1618315$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Krishnamoorthi, Ramaswamy</creatorcontrib><creatorcontrib>Nemmers, Sylvia</creatorcontrib><creatorcontrib>Tobias, Brian</creatorcontrib><title>Natural abundance 15N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>15N NMR assignments were made to the backbone amide nitrogen atoms at natural isotopic abundance of intact and reactive-site (Arg
5—Ile
6) hydrolyzed
Cucurbita maxima trypsin inhibitor III (CMTI-III and CMTI-III*, respectively) by means of 2D proton-detected heteronuclear single bond chemical shift correlation (HSBC) spectroscopy, utilizing the previously made sequence-specific
1H NMR assignments (Krishnamoorthi et al. (1992) Biochemistry 31. 898–904). Comparison of the
15N chemical shifts of the two forms of the inhibitor molecule revealed significant changes not only for residues located near the reactive-site region, but also for those distantly located. Residues Cys
3, Arg
5, Leu
7, Met
8, Cys
10, Cys
16, Glu
19, His
25, Tyr
27, Cys
28 and Gly
28 showed significant chemical shift changes ranging from 0.3 to 6.1 ppm, thus indicating structural perturbations that were transmitted throughout the molecule. These findings confirm the earlier conclusions based on
1H NMR investigations.</description><subject>1H— 15N chemical shift correlation</subject><subject>Activated Hageman factor</subject><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation</subject><subject>CMTI</subject><subject>Cucurbita maxima</subject><subject>Cucurbita maxima trypsin inhibitor</subject><subject>Disaccharides</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucans</subject><subject>heteronuclear single bond chemical shift correlation spectroscopy</subject><subject>high-performance liquid chromatography</subject><subject>HPLC</subject><subject>HSBC</subject><subject>Hydrolases</subject><subject>Hydrolysis</subject><subject>Inhibitor</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular Sequence Data</subject><subject>NMR</subject><subject>nuclear magnetic resonance</subject><subject>parts per million</subject><subject>Peptide Fragments - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Plants, Edible - chemistry</subject><subject>ppm</subject><subject>Pumpkin</subject><subject>Serine protease</subject><subject>Trypsin</subject><subject>Trypsin Inhibitors - chemistry</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNp9UcmKFDEYDqKM7egbKOQgoofSLJVaLoI201owtiB6Dln-OJFa2iQ1Y_kmvq2p6Wa8eUrybYTvQ-gpJa8podUbQmhZiLrlL1v2qiEVqYvuHtrQpuYFL6vmPtrcSR6iRzH-IPnd0PYMndGKNpyKDfqzV2kOqsdKz6NVowFMxR7vP33BKkb_fRxgTBFb6P0IKgGOKczmaLHeOQiQPRFrSDcAI_ZjUiZhNVocIN_8NRTRZ9_VYsPUL7_B4u1s5qB9UnhQv_ygcArLIfrVfOUzPgXcdd1j9MCpPsKT03mOvu0uvm4_FpefP3Tbd5cFMEK6wopWaTDGmVIozR1lLTMN08RxLrRmjePasVIboWltnWhBGG6ZsgDgmgb4OXpxzD2E6ecMMcnBRwN9r0aY5ihrTkrRVnUWPjsJZz2AlYeQ_x4Weeoy889PvIpG9S7kNn28kwlOW1LyLNsdZTe-h-VfCpHrqnKdTK6TyZbJ21VlJ3cX79lKrHjLbtEuB709BkFu59pDkNH4dQ3rA5gk7eT_m8r_AufNr7Y</recordid><startdate>19920615</startdate><enddate>19920615</enddate><creator>Krishnamoorthi, Ramaswamy</creator><creator>Nemmers, Sylvia</creator><creator>Tobias, Brian</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19920615</creationdate><title>Natural abundance 15N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III</title><author>Krishnamoorthi, Ramaswamy ; Nemmers, Sylvia ; Tobias, Brian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e200I-d59abeccfc45ab3f1292c82b0f335bb28f3bf24bc5b17df59e5c3d2adeeef88e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>1H— 15N chemical shift correlation</topic><topic>Activated Hageman factor</topic><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation</topic><topic>CMTI</topic><topic>Cucurbita maxima</topic><topic>Cucurbita maxima trypsin inhibitor</topic><topic>Disaccharides</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glucans</topic><topic>heteronuclear single bond chemical shift correlation spectroscopy</topic><topic>high-performance liquid chromatography</topic><topic>HPLC</topic><topic>HSBC</topic><topic>Hydrolases</topic><topic>Hydrolysis</topic><topic>Inhibitor</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular Sequence Data</topic><topic>NMR</topic><topic>nuclear magnetic resonance</topic><topic>parts per million</topic><topic>Peptide Fragments - chemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Plants, Edible - chemistry</topic><topic>ppm</topic><topic>Pumpkin</topic><topic>Serine protease</topic><topic>Trypsin</topic><topic>Trypsin Inhibitors - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Krishnamoorthi, Ramaswamy</creatorcontrib><creatorcontrib>Nemmers, Sylvia</creatorcontrib><creatorcontrib>Tobias, Brian</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Krishnamoorthi, Ramaswamy</au><au>Nemmers, Sylvia</au><au>Tobias, Brian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Natural abundance 15N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1992-06-15</date><risdate>1992</risdate><volume>304</volume><issue>2</issue><spage>149</spage><epage>152</epage><pages>149-152</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>15N NMR assignments were made to the backbone amide nitrogen atoms at natural isotopic abundance of intact and reactive-site (Arg
5—Ile
6) hydrolyzed
Cucurbita maxima trypsin inhibitor III (CMTI-III and CMTI-III*, respectively) by means of 2D proton-detected heteronuclear single bond chemical shift correlation (HSBC) spectroscopy, utilizing the previously made sequence-specific
1H NMR assignments (Krishnamoorthi et al. (1992) Biochemistry 31. 898–904). Comparison of the
15N chemical shifts of the two forms of the inhibitor molecule revealed significant changes not only for residues located near the reactive-site region, but also for those distantly located. Residues Cys
3, Arg
5, Leu
7, Met
8, Cys
10, Cys
16, Glu
19, His
25, Tyr
27, Cys
28 and Gly
28 showed significant chemical shift changes ranging from 0.3 to 6.1 ppm, thus indicating structural perturbations that were transmitted throughout the molecule. These findings confirm the earlier conclusions based on
1H NMR investigations.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>1618315</pmid><doi>10.1016/0014-5793(92)80607-I</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1992-06, Vol.304 (2), p.149-152 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| subjects | 1H— 15N chemical shift correlation Activated Hageman factor Amino Acid Sequence Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Blood coagulation CMTI Cucurbita maxima Cucurbita maxima trypsin inhibitor Disaccharides Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Glucans heteronuclear single bond chemical shift correlation spectroscopy high-performance liquid chromatography HPLC HSBC Hydrolases Hydrolysis Inhibitor Magnetic Resonance Spectroscopy Molecular Sequence Data NMR nuclear magnetic resonance parts per million Peptide Fragments - chemistry Plant Proteins - chemistry Plants, Edible - chemistry ppm Pumpkin Serine protease Trypsin Trypsin Inhibitors - chemistry |
| title | Natural abundance 15N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III |
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