NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride
Understanding protein folding requires complete characterization of all the states of the protein present along the folding pathways. For this purpose nuclear magnetic resonance (NMR) has proved to be a very powerful technique because of the great detail it can unravel regarding the structure and dy...
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| Veröffentlicht in: | FEBS letters 2001-12, Vol.509 (2), p.218-224 |
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| creator | Bhavesh, Neel S Panchal, Sanjay C Mittal, Rohit Hosur, Ramakrishna V |
| description | Understanding protein folding requires complete characterization of all the states of the protein present along the folding pathways. For this purpose nuclear magnetic resonance (NMR) has proved to be a very powerful technique because of the great detail it can unravel regarding the structure and dynamics of protein molecules. We report here NMR identification of local structural preferences in human immunodeficiency virus-1 protease in the ‘unfolded state’. Analyses of the chemical shifts revealed the presence of local structural preferences many of which are native-like, and there are also some non-native structural elements. Three-bond H
N–H
α coupling constants that could be measured for some of the N-terminal and C-terminal residues are consistent with the native-like β-structure. Unusually shifted
15N and amide proton chemical shifts of residues adjacent to some prolines and tryptophans also indicate the presence of some structural elements. These conclusions are supported by amide proton temperature coefficients and nuclear Overhauser enhancement data. The locations of the residues exhibiting preferred structural propensities on the crystal structure of the protein, give useful insights into the folding mechanism of this protein. |
| doi_str_mv | 10.1016/S0014-5793(01)03066-6 |
| format | Article |
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N–H
α coupling constants that could be measured for some of the N-terminal and C-terminal residues are consistent with the native-like β-structure. Unusually shifted
15N and amide proton chemical shifts of residues adjacent to some prolines and tryptophans also indicate the presence of some structural elements. These conclusions are supported by amide proton temperature coefficients and nuclear Overhauser enhancement data. The locations of the residues exhibiting preferred structural propensities on the crystal structure of the protein, give useful insights into the folding mechanism of this protein.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)03066-6</identifier><identifier>PMID: 11741592</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>AIDS, acquired immunodeficiency syndrome ; Backbone resonance assignment ; Denatured/unfolded protein ; Dimerization ; Guanidine ; Guanidine hydrochloride ; HIV Protease - chemistry ; HIV, human immunodeficiency virus ; HIV-1 - enzymology ; HN(C)N ; HNN ; HSQC, heteronuclear single quantum coherence ; Human immunodeficiency virus-1 protease ; Models, Molecular ; NMR, nuclear magnetic resonance ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular ; Protein Denaturation ; Protein Folding ; Protein Structure, Secondary ; Residual structural propensity ; TROSY, transverse relaxation-optimized spectroscopy</subject><ispartof>FEBS letters, 2001-12, Vol.509 (2), p.218-224</ispartof><rights>2001</rights><rights>FEBS Letters 509 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4576-b64b2811f3f65e7a33005cd9a5c962d25b517540c2fd55d06ef6ff0f7bc2fb7d3</citedby><cites>FETCH-LOGICAL-c4576-b64b2811f3f65e7a33005cd9a5c962d25b517540c2fd55d06ef6ff0f7bc2fb7d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2801%2903066-6$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0014-5793(01)03066-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3536,27903,27904,45553,45554,45974,46388,46812</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11741592$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bhavesh, Neel S</creatorcontrib><creatorcontrib>Panchal, Sanjay C</creatorcontrib><creatorcontrib>Mittal, Rohit</creatorcontrib><creatorcontrib>Hosur, Ramakrishna V</creatorcontrib><title>NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Understanding protein folding requires complete characterization of all the states of the protein present along the folding pathways. For this purpose nuclear magnetic resonance (NMR) has proved to be a very powerful technique because of the great detail it can unravel regarding the structure and dynamics of protein molecules. We report here NMR identification of local structural preferences in human immunodeficiency virus-1 protease in the ‘unfolded state’. Analyses of the chemical shifts revealed the presence of local structural preferences many of which are native-like, and there are also some non-native structural elements. Three-bond H
N–H
α coupling constants that could be measured for some of the N-terminal and C-terminal residues are consistent with the native-like β-structure. Unusually shifted
15N and amide proton chemical shifts of residues adjacent to some prolines and tryptophans also indicate the presence of some structural elements. These conclusions are supported by amide proton temperature coefficients and nuclear Overhauser enhancement data. The locations of the residues exhibiting preferred structural propensities on the crystal structure of the protein, give useful insights into the folding mechanism of this protein.</description><subject>AIDS, acquired immunodeficiency syndrome</subject><subject>Backbone resonance assignment</subject><subject>Denatured/unfolded protein</subject><subject>Dimerization</subject><subject>Guanidine</subject><subject>Guanidine hydrochloride</subject><subject>HIV Protease - chemistry</subject><subject>HIV, human immunodeficiency virus</subject><subject>HIV-1 - enzymology</subject><subject>HN(C)N</subject><subject>HNN</subject><subject>HSQC, heteronuclear single quantum coherence</subject><subject>Human immunodeficiency virus-1 protease</subject><subject>Models, Molecular</subject><subject>NMR, nuclear magnetic resonance</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Protein Denaturation</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Residual structural propensity</subject><subject>TROSY, transverse relaxation-optimized spectroscopy</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi0EokvhJ4B8QnAIeOLYTk4Iqpat1ILE19VK7DFrlI1b2wH23-PsruBYTh7PPPOh9yXkKbBXwEC-_swYNJVQHX_B4CXjTMpK3iMraBWveCPb-2T1Fzkhj1L6wcq_he4hOQFQDYiuXpHfH64_UW9xyt5502cfJhocHYPpR5pynE2eYwlvIjqMOBlM1E90ffmtgpIMGfuENGPelKqlG8wYg_VbjAsm6TX9PveTt35CutnZGMxmDLEsfEweuH5M-OT4npKvF-dfztbV1cf3l2dvryrTCCWrQTZD3QI47qRA1XPOmDC264XpZG1rMQhQomGmdlYIyyQ66RxzaiiZQVl-Sp4f5pZjb2dMWW99MjiO_YRhTlrVXBU92Z0gtFK1IHgBxQE0MaRUdNE30W_7uNPA9OKN3nujF-E1A733RsvS9-y4YB62aP91Hc0owPoA_PIj7v5vqr44f1fvK0uBwT697HpzGIVF2p8eo07GL-5ZH9FkbYO_49o_uYizCQ</recordid><startdate>20011207</startdate><enddate>20011207</enddate><creator>Bhavesh, Neel S</creator><creator>Panchal, Sanjay C</creator><creator>Mittal, Rohit</creator><creator>Hosur, Ramakrishna V</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20011207</creationdate><title>NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride</title><author>Bhavesh, Neel S ; Panchal, Sanjay C ; Mittal, Rohit ; Hosur, Ramakrishna V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4576-b64b2811f3f65e7a33005cd9a5c962d25b517540c2fd55d06ef6ff0f7bc2fb7d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>AIDS, acquired immunodeficiency syndrome</topic><topic>Backbone resonance assignment</topic><topic>Denatured/unfolded protein</topic><topic>Dimerization</topic><topic>Guanidine</topic><topic>Guanidine hydrochloride</topic><topic>HIV Protease - chemistry</topic><topic>HIV, human immunodeficiency virus</topic><topic>HIV-1 - enzymology</topic><topic>HN(C)N</topic><topic>HNN</topic><topic>HSQC, heteronuclear single quantum coherence</topic><topic>Human immunodeficiency virus-1 protease</topic><topic>Models, Molecular</topic><topic>NMR, nuclear magnetic resonance</topic><topic>Nuclear magnetic resonance</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Protein Denaturation</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Residual structural propensity</topic><topic>TROSY, transverse relaxation-optimized spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bhavesh, Neel S</creatorcontrib><creatorcontrib>Panchal, Sanjay C</creatorcontrib><creatorcontrib>Mittal, Rohit</creatorcontrib><creatorcontrib>Hosur, Ramakrishna V</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bhavesh, Neel S</au><au>Panchal, Sanjay C</au><au>Mittal, Rohit</au><au>Hosur, Ramakrishna V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-12-07</date><risdate>2001</risdate><volume>509</volume><issue>2</issue><spage>218</spage><epage>224</epage><pages>218-224</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Understanding protein folding requires complete characterization of all the states of the protein present along the folding pathways. For this purpose nuclear magnetic resonance (NMR) has proved to be a very powerful technique because of the great detail it can unravel regarding the structure and dynamics of protein molecules. We report here NMR identification of local structural preferences in human immunodeficiency virus-1 protease in the ‘unfolded state’. Analyses of the chemical shifts revealed the presence of local structural preferences many of which are native-like, and there are also some non-native structural elements. Three-bond H
N–H
α coupling constants that could be measured for some of the N-terminal and C-terminal residues are consistent with the native-like β-structure. Unusually shifted
15N and amide proton chemical shifts of residues adjacent to some prolines and tryptophans also indicate the presence of some structural elements. These conclusions are supported by amide proton temperature coefficients and nuclear Overhauser enhancement data. The locations of the residues exhibiting preferred structural propensities on the crystal structure of the protein, give useful insights into the folding mechanism of this protein.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11741592</pmid><doi>10.1016/S0014-5793(01)03066-6</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Journals Frontfile Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | AIDS, acquired immunodeficiency syndrome Backbone resonance assignment Denatured/unfolded protein Dimerization Guanidine Guanidine hydrochloride HIV Protease - chemistry HIV, human immunodeficiency virus HIV-1 - enzymology HN(C)N HNN HSQC, heteronuclear single quantum coherence Human immunodeficiency virus-1 protease Models, Molecular NMR, nuclear magnetic resonance Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Protein Denaturation Protein Folding Protein Structure, Secondary Residual structural propensity TROSY, transverse relaxation-optimized spectroscopy |
| title | NMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride |
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