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dc.creatorVaquero, Vanesaen_US
dc.creatorPratt, David W.en_US
dc.date.accessioned2011-07-12T17:39:53Z
dc.date.available2011-07-12T17:39:53Z
dc.date.issued2011en_US
dc.identifier2011-MH-11en_US
dc.identifier.urihttp://hdl.handle.net/1811/49686
dc.descriptionWork supported by NSF(CHE-0911117).en_US
dc.descriptionAuthor Institution: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260en_US
dc.description.abstractChirped pulse Fourier Transform microwave spectroscopy can be used to study either the structure of heavy biomolecular related compounds or the complex landscape of more simple molecules. Protected amino acids are the key to understand how the different interactions between the amino and the carboxylic groups can govern the folding process of peptides to yield either $\alpha$-helix or $\beta$-sheet related structures. In this work, the aromatic amino acid phenylalanine protected in both, amino and carboxylic groups, has been studied revealing its preferential structure and confirming the structure found by Gerhards. D-threoninol is an acyclic diol which can be used as a building block to form a double-helical structure similar to the one from the natural nucleic acids. The result is called acyclic threoninol nucleic acid (\textit{a}TNA), which shows a high compatibility with the DNA strands. Here the conformational preferences of the D-threoninol in gas phase are reported for which several conformers have been found in the molecular beam.en_US
dc.language.isoenen_US
dc.publisherOhio State Universityen_US
dc.titleTHE ROTATIONAL SPECTRUM OF BIOMOLECULAR RELATED COMPOUNDSen_US
dc.typeArticleen_US


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