Revealing the multiple structures of serine
We explored the conformational landscape of the proteinogenic amino acid serine [CH₂OHFormula CH(NH₂)Formula COOH] in the gas phase. Solid serine was vaporized by laser ablation, expanded in a supersonic jet, and characterized by Fourier transform microwave spectroscopy. In the isolation conditions...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2007-12, Vol.104 (51), p.20183-20188 |
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| container_issue | 51 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Blanco, Susana Sanz, M. Eugenia López, Juan C Alonso, José L |
| description | We explored the conformational landscape of the proteinogenic amino acid serine [CH₂OHFormula CH(NH₂)Formula COOH] in the gas phase. Solid serine was vaporized by laser ablation, expanded in a supersonic jet, and characterized by Fourier transform microwave spectroscopy. In the isolation conditions of the jet there have been discovered up to seven different neutral (non-zwitterionic) structures of serine, which are conclusively identified by the comparison between the experimental values of the rotational and quadrupole coupling constants with those predicted by ab initio calculations. These seven forms can serve as a basis to represent the shape of serine in the gas phase. From the postexpansion abundances we derived the conformational stability trend, which is controlled by the subtle network of intramolecular hydrogen bonds formed between the polar groups in the amino acid backbone and the hydroxy side chain. It is proposed that conformational cooling perturbs the equilibrium conformational distribution; thus, some of the lower-energy forms are "missing" in the supersonic expansion. |
| doi_str_mv | 10.1073/pnas.0705676104 |
| format | Article |
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Eugenia ; López, Juan C ; Alonso, José L</creator><creatorcontrib>Blanco, Susana ; Sanz, M. Eugenia ; López, Juan C ; Alonso, José L</creatorcontrib><description>We explored the conformational landscape of the proteinogenic amino acid serine [CH₂OHFormula CH(NH₂)Formula COOH] in the gas phase. Solid serine was vaporized by laser ablation, expanded in a supersonic jet, and characterized by Fourier transform microwave spectroscopy. In the isolation conditions of the jet there have been discovered up to seven different neutral (non-zwitterionic) structures of serine, which are conclusively identified by the comparison between the experimental values of the rotational and quadrupole coupling constants with those predicted by ab initio calculations. These seven forms can serve as a basis to represent the shape of serine in the gas phase. From the postexpansion abundances we derived the conformational stability trend, which is controlled by the subtle network of intramolecular hydrogen bonds formed between the polar groups in the amino acid backbone and the hydroxy side chain. It is proposed that conformational cooling perturbs the equilibrium conformational distribution; thus, some of the lower-energy forms are "missing" in the supersonic expansion.</description><identifier>ISSN: 0027-8424</identifier><identifier>ISSN: 1091-6490</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0705676104</identifier><identifier>PMID: 18077350</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino acids ; Atomic interactions ; Atoms ; Biochemistry ; Biological Sciences ; Fourier transforms ; Hydrogen ; Hydrogen Bonding ; Hydrogen bonds ; Lasers ; Microwaves ; Molecular Conformation ; Molecular Structure ; Phase Transition ; Physical Sciences ; Quadrupoles ; Rotational spectra ; Serine - chemistry ; Spectroscopy ; Spectrum analysis ; Vapor phases</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2007-12, Vol.104 (51), p.20183-20188</ispartof><rights>Copyright 2007 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Dec 18, 2007</rights><rights>2007 by The National Academy of Sciences of the USA</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c550t-5934ae6b84dd810a83940d2575ba2fd69a6ca97b4f3d47a06a6262f3bcb84a493</citedby><cites>FETCH-LOGICAL-c550t-5934ae6b84dd810a83940d2575ba2fd69a6ca97b4f3d47a06a6262f3bcb84a493</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/104/51.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/25450866$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/25450866$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18077350$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blanco, Susana</creatorcontrib><creatorcontrib>Sanz, M. Eugenia</creatorcontrib><creatorcontrib>López, Juan C</creatorcontrib><creatorcontrib>Alonso, José L</creatorcontrib><title>Revealing the multiple structures of serine</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We explored the conformational landscape of the proteinogenic amino acid serine [CH₂OHFormula CH(NH₂)Formula COOH] in the gas phase. Solid serine was vaporized by laser ablation, expanded in a supersonic jet, and characterized by Fourier transform microwave spectroscopy. In the isolation conditions of the jet there have been discovered up to seven different neutral (non-zwitterionic) structures of serine, which are conclusively identified by the comparison between the experimental values of the rotational and quadrupole coupling constants with those predicted by ab initio calculations. These seven forms can serve as a basis to represent the shape of serine in the gas phase. From the postexpansion abundances we derived the conformational stability trend, which is controlled by the subtle network of intramolecular hydrogen bonds formed between the polar groups in the amino acid backbone and the hydroxy side chain. It is proposed that conformational cooling perturbs the equilibrium conformational distribution; thus, some of the lower-energy forms are "missing" in the supersonic expansion.</description><subject>Amino acids</subject><subject>Atomic interactions</subject><subject>Atoms</subject><subject>Biochemistry</subject><subject>Biological Sciences</subject><subject>Fourier transforms</subject><subject>Hydrogen</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Lasers</subject><subject>Microwaves</subject><subject>Molecular Conformation</subject><subject>Molecular Structure</subject><subject>Phase Transition</subject><subject>Physical Sciences</subject><subject>Quadrupoles</subject><subject>Rotational spectra</subject><subject>Serine - chemistry</subject><subject>Spectroscopy</subject><subject>Spectrum analysis</subject><subject>Vapor phases</subject><issn>0027-8424</issn><issn>1091-6490</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0Utr3DAUBWBRWppp2nVXSU0XgVKcXL2lTaGE9AGBQtushWzLEw8aayLJIf33kZkh02STlRf3u0e-HITeYzjFIOnZZrTpFCRwIQUG9gItMGhcC6bhJVoAEFkrRtgBepPSCgA0V_AaHWAFUlIOC_T5t7t11g_jssrXrlpPPg8b76qU49TmKbpUhb5KLg6je4te9dYn9273PURX3y7-nv-oL399_3n-9bJuOYdcc02ZdaJRrOsUBquoZtARLnljSd8JbUVrtWxYTzsmLQgriCA9bdqyYpmmh-jLNnczNWvXtW7M0XqzicPaxn8m2ME8nozDtVmGW0MwZwx4CTjZBcRwM7mUzXpIrfPeji5MyQgNUjMiC_z4BK7CFMdynCGAqdQK0-cQk1irgs62qI0hpej6h9_FYOaqzFyV2VdVNo7_v3Lvd90U8GkH5s19HDMczy8ravrJ--zucrHVM7aQoy1ZpRzigyGccVBClPmH7by3wdhlHJK5-jMfCFAaFAD0HlZcuXU</recordid><startdate>20071218</startdate><enddate>20071218</enddate><creator>Blanco, Susana</creator><creator>Sanz, M. 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Eugenia</au><au>López, Juan C</au><au>Alonso, José L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Revealing the multiple structures of serine</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2007-12-18</date><risdate>2007</risdate><volume>104</volume><issue>51</issue><spage>20183</spage><epage>20188</epage><pages>20183-20188</pages><issn>0027-8424</issn><issn>1091-6490</issn><eissn>1091-6490</eissn><abstract>We explored the conformational landscape of the proteinogenic amino acid serine [CH₂OHFormula CH(NH₂)Formula COOH] in the gas phase. Solid serine was vaporized by laser ablation, expanded in a supersonic jet, and characterized by Fourier transform microwave spectroscopy. In the isolation conditions of the jet there have been discovered up to seven different neutral (non-zwitterionic) structures of serine, which are conclusively identified by the comparison between the experimental values of the rotational and quadrupole coupling constants with those predicted by ab initio calculations. These seven forms can serve as a basis to represent the shape of serine in the gas phase. From the postexpansion abundances we derived the conformational stability trend, which is controlled by the subtle network of intramolecular hydrogen bonds formed between the polar groups in the amino acid backbone and the hydroxy side chain. 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| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino acids Atomic interactions Atoms Biochemistry Biological Sciences Fourier transforms Hydrogen Hydrogen Bonding Hydrogen bonds Lasers Microwaves Molecular Conformation Molecular Structure Phase Transition Physical Sciences Quadrupoles Rotational spectra Serine - chemistry Spectroscopy Spectrum analysis Vapor phases |
| title | Revealing the multiple structures of serine |
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