Orientation and dynamics of transmembrane peptides: the power of simple models
In this review we discuss recent insights obtained from well-characterized model systems into the factors that determine the orientation and tilt angles of transmembrane peptides in lipid bilayers. We will compare tilt angles of synthetic peptides with those of natural peptides and proteins, and we...
Gespeichert in:
| Veröffentlicht in: | European biophysics journal 2010-03, Vol.39 (4), p.609-621 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 621 |
|---|---|
| container_issue | 4 |
| container_start_page | 609 |
| container_title | European biophysics journal |
| container_volume | 39 |
| creator | Holt, Andrea Killian, J. Antoinette |
| description | In this review we discuss recent insights obtained from well-characterized model systems into the factors that determine the orientation and tilt angles of transmembrane peptides in lipid bilayers. We will compare tilt angles of synthetic peptides with those of natural peptides and proteins, and we will discuss how tilt can be modulated by hydrophobic mismatch between the thickness of the bilayer and the length of the membrane spanning part of the peptide or protein. In particular, we will focus on results obtained on tryptophan-flanked model peptides (WALP peptides) as a case study to illustrate possible consequences of hydrophobic mismatch in molecular detail and to highlight the importance of peptide dynamics for the experimental determination of tilt angles. We will conclude with discussing some future prospects and challenges concerning the use of simple peptide/lipid model systems as a tool to understand membrane structure and function. |
| doi_str_mv | 10.1007/s00249-009-0567-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2841270</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>733183905</sourcerecordid><originalsourceid>FETCH-LOGICAL-c558t-7381db50e985b27f5a393e07c4cfaa2abd87d0810d6c30101e5506bfa71a58b53</originalsourceid><addsrcrecordid>eNp9UcFu1TAQtBCofZR-ABeIuPQUumvHzw6HSqgqFKmih9Kz5cTOq6skTu08UP---5RSoAcO9mq1M7MeD2NvET4igDrOALyqSwA6cq1KfMFWWAleIqB6yVZ0y1JJhfvsdc63AJVE1HtsnxMRkPMV-36Zgh9nO4c4FnZ0hbsf7RDaXMSumJMd8-CHhqovJj_Nwfn8qZhvqIu_fNqBchim3hdDdL7Pb9irzvbZHz7WA3b95ezH6Xl5cfn12-nni7KVUs-lEhpdI8HXWjZcddKKWnhQbdV21nLbOK0caAS3bgWQGy8lrJvOKrRSN1IcsJNFd9o2g3ctWUi2N1MKg033Jtpg_p2M4cZs4k_DdYVcAQkcPQqkeLf1eTZDyK3ve3Iat9koIVCLGnarPjxD3sZtGsmd4bwGLmuxJhAuoDbFnJPvnp6CYHZZmSUrQ1mZXVYGifPubw9PjN_hEIAvgEyjcePTn83_U32_kDobjd2kkM31FenRN2okV7V4APohqLc</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>229025936</pqid></control><display><type>article</type><title>Orientation and dynamics of transmembrane peptides: the power of simple models</title><source>MEDLINE</source><source>SpringerLink Journals</source><creator>Holt, Andrea ; Killian, J. Antoinette</creator><creatorcontrib>Holt, Andrea ; Killian, J. Antoinette</creatorcontrib><description>In this review we discuss recent insights obtained from well-characterized model systems into the factors that determine the orientation and tilt angles of transmembrane peptides in lipid bilayers. We will compare tilt angles of synthetic peptides with those of natural peptides and proteins, and we will discuss how tilt can be modulated by hydrophobic mismatch between the thickness of the bilayer and the length of the membrane spanning part of the peptide or protein. In particular, we will focus on results obtained on tryptophan-flanked model peptides (WALP peptides) as a case study to illustrate possible consequences of hydrophobic mismatch in molecular detail and to highlight the importance of peptide dynamics for the experimental determination of tilt angles. We will conclude with discussing some future prospects and challenges concerning the use of simple peptide/lipid model systems as a tool to understand membrane structure and function.</description><identifier>ISSN: 0175-7571</identifier><identifier>EISSN: 1432-1017</identifier><identifier>DOI: 10.1007/s00249-009-0567-1</identifier><identifier>PMID: 20020122</identifier><language>eng</language><publisher>Berlin/Heidelberg: Berlin/Heidelberg : Springer-Verlag</publisher><subject>Amino Acid Sequence ; Biochemistry ; Biological and Medical Physics ; Biomedical and Life Sciences ; Biophysics ; Cell Biology ; Cell Membrane - chemistry ; Cell Membrane - metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Life Sciences ; Membrane Biology ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Membranes ; Models, Molecular ; Molecular Sequence Data ; Nanotechnology ; Neurobiology ; Peptides ; Peptides - chemistry ; Peptides - metabolism ; Protein Structure, Secondary ; Review</subject><ispartof>European biophysics journal, 2010-03, Vol.39 (4), p.609-621</ispartof><rights>The Author(s) 2009</rights><rights>European Biophysical Societies' Association 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c558t-7381db50e985b27f5a393e07c4cfaa2abd87d0810d6c30101e5506bfa71a58b53</citedby><cites>FETCH-LOGICAL-c558t-7381db50e985b27f5a393e07c4cfaa2abd87d0810d6c30101e5506bfa71a58b53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00249-009-0567-1$$EPDF$$P50$$Gspringer$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00249-009-0567-1$$EHTML$$P50$$Gspringer$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20020122$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Holt, Andrea</creatorcontrib><creatorcontrib>Killian, J. Antoinette</creatorcontrib><title>Orientation and dynamics of transmembrane peptides: the power of simple models</title><title>European biophysics journal</title><addtitle>Eur Biophys J</addtitle><addtitle>Eur Biophys J</addtitle><description>In this review we discuss recent insights obtained from well-characterized model systems into the factors that determine the orientation and tilt angles of transmembrane peptides in lipid bilayers. We will compare tilt angles of synthetic peptides with those of natural peptides and proteins, and we will discuss how tilt can be modulated by hydrophobic mismatch between the thickness of the bilayer and the length of the membrane spanning part of the peptide or protein. In particular, we will focus on results obtained on tryptophan-flanked model peptides (WALP peptides) as a case study to illustrate possible consequences of hydrophobic mismatch in molecular detail and to highlight the importance of peptide dynamics for the experimental determination of tilt angles. We will conclude with discussing some future prospects and challenges concerning the use of simple peptide/lipid model systems as a tool to understand membrane structure and function.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biological and Medical Physics</subject><subject>Biomedical and Life Sciences</subject><subject>Biophysics</subject><subject>Cell Biology</subject><subject>Cell Membrane - chemistry</subject><subject>Cell Membrane - metabolism</subject><subject>Humans</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Membranes</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Nanotechnology</subject><subject>Neurobiology</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Protein Structure, Secondary</subject><subject>Review</subject><issn>0175-7571</issn><issn>1432-1017</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9UcFu1TAQtBCofZR-ABeIuPQUumvHzw6HSqgqFKmih9Kz5cTOq6skTu08UP---5RSoAcO9mq1M7MeD2NvET4igDrOALyqSwA6cq1KfMFWWAleIqB6yVZ0y1JJhfvsdc63AJVE1HtsnxMRkPMV-36Zgh9nO4c4FnZ0hbsf7RDaXMSumJMd8-CHhqovJj_Nwfn8qZhvqIu_fNqBchim3hdDdL7Pb9irzvbZHz7WA3b95ezH6Xl5cfn12-nni7KVUs-lEhpdI8HXWjZcddKKWnhQbdV21nLbOK0caAS3bgWQGy8lrJvOKrRSN1IcsJNFd9o2g3ctWUi2N1MKg033Jtpg_p2M4cZs4k_DdYVcAQkcPQqkeLf1eTZDyK3ve3Iat9koIVCLGnarPjxD3sZtGsmd4bwGLmuxJhAuoDbFnJPvnp6CYHZZmSUrQ1mZXVYGifPubw9PjN_hEIAvgEyjcePTn83_U32_kDobjd2kkM31FenRN2okV7V4APohqLc</recordid><startdate>20100301</startdate><enddate>20100301</enddate><creator>Holt, Andrea</creator><creator>Killian, J. Antoinette</creator><general>Berlin/Heidelberg : Springer-Verlag</general><general>Springer-Verlag</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>C6C</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>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</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>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</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>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100301</creationdate><title>Orientation and dynamics of transmembrane peptides: the power of simple models</title><author>Holt, Andrea ; Killian, J. Antoinette</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c558t-7381db50e985b27f5a393e07c4cfaa2abd87d0810d6c30101e5506bfa71a58b53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Biochemistry</topic><topic>Biological and Medical Physics</topic><topic>Biomedical and Life Sciences</topic><topic>Biophysics</topic><topic>Cell Biology</topic><topic>Cell Membrane - chemistry</topic><topic>Cell Membrane - metabolism</topic><topic>Humans</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Life Sciences</topic><topic>Membrane Biology</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Membranes</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Nanotechnology</topic><topic>Neurobiology</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Protein Structure, Secondary</topic><topic>Review</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Holt, Andrea</creatorcontrib><creatorcontrib>Killian, J. Antoinette</creatorcontrib><collection>AGRIS</collection><collection>Springer Nature OA Free Journals</collection><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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</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>Technology Research 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>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</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>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</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>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>European biophysics journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Holt, Andrea</au><au>Killian, J. Antoinette</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Orientation and dynamics of transmembrane peptides: the power of simple models</atitle><jtitle>European biophysics journal</jtitle><stitle>Eur Biophys J</stitle><addtitle>Eur Biophys J</addtitle><date>2010-03-01</date><risdate>2010</risdate><volume>39</volume><issue>4</issue><spage>609</spage><epage>621</epage><pages>609-621</pages><issn>0175-7571</issn><eissn>1432-1017</eissn><abstract>In this review we discuss recent insights obtained from well-characterized model systems into the factors that determine the orientation and tilt angles of transmembrane peptides in lipid bilayers. We will compare tilt angles of synthetic peptides with those of natural peptides and proteins, and we will discuss how tilt can be modulated by hydrophobic mismatch between the thickness of the bilayer and the length of the membrane spanning part of the peptide or protein. In particular, we will focus on results obtained on tryptophan-flanked model peptides (WALP peptides) as a case study to illustrate possible consequences of hydrophobic mismatch in molecular detail and to highlight the importance of peptide dynamics for the experimental determination of tilt angles. We will conclude with discussing some future prospects and challenges concerning the use of simple peptide/lipid model systems as a tool to understand membrane structure and function.</abstract><cop>Berlin/Heidelberg</cop><pub>Berlin/Heidelberg : Springer-Verlag</pub><pmid>20020122</pmid><doi>10.1007/s00249-009-0567-1</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0175-7571 |
| ispartof | European biophysics journal, 2010-03, Vol.39 (4), p.609-621 |
| issn | 0175-7571 1432-1017 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2841270 |
| source | MEDLINE; SpringerLink Journals |
| subjects | Amino Acid Sequence Biochemistry Biological and Medical Physics Biomedical and Life Sciences Biophysics Cell Biology Cell Membrane - chemistry Cell Membrane - metabolism Humans Hydrophobic and Hydrophilic Interactions Life Sciences Membrane Biology Membrane Proteins - chemistry Membrane Proteins - metabolism Membranes Models, Molecular Molecular Sequence Data Nanotechnology Neurobiology Peptides Peptides - chemistry Peptides - metabolism Protein Structure, Secondary Review |
| title | Orientation and dynamics of transmembrane peptides: the power of simple models |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-26T07%3A07%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Orientation%20and%20dynamics%20of%20transmembrane%20peptides:%20the%20power%20of%20simple%20models&rft.jtitle=European%20biophysics%20journal&rft.au=Holt,%20Andrea&rft.date=2010-03-01&rft.volume=39&rft.issue=4&rft.spage=609&rft.epage=621&rft.pages=609-621&rft.issn=0175-7571&rft.eissn=1432-1017&rft_id=info:doi/10.1007/s00249-009-0567-1&rft_dat=%3Cproquest_pubme%3E733183905%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=229025936&rft_id=info:pmid/20020122&rfr_iscdi=true |