Espectroscopia Raman de cristais de DL-norleucina em altas pressões
| Ano de defesa: | 2022 |
|---|---|
| Autor(a) principal: | |
| Orientador(a): | |
| Banca de defesa: | |
| Tipo de documento: | Dissertação |
| Tipo de acesso: | Acesso aberto |
| Idioma: | por |
| Instituição de defesa: |
Não Informado pela instituição
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| Programa de Pós-Graduação: |
Não Informado pela instituição
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| Departamento: |
Não Informado pela instituição
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| País: |
Não Informado pela instituição
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| Palavras-chave em Português: | |
| Link de acesso: | http://www.repositorio.ufc.br/handle/riufc/64189 |
Resumo: | Amino acids are the basic building blocks of proteins, which are indispensable for life. In the solid state, the stability of the structure is mainly maintained by hydrogen bonding that occurs between the nitrogen of the amino group and the oxygen of the carboxylic group. Mainly due to the versatility of their structures, amino acids can form polymorphic structures, bind to other amino acids forming dipeptides or even to other molecules and atoms such as: metals, organic and inorganic molecules, forming salts and metallics creating new materials with properties different from those of pure amino acids and even in some cases with potential technological applications mainly non-linear optical properties with potential applicability in electronic devices and pharmaceutical industry. Numerous works have been described in the study of the stability of the structure of amino acids both as a function of pressure and temperature. Several phase transitions have been reported. In this work we present a study by Raman spectroscopy of the DL-norleucine crystal as a function of the hydrostatic pressure varying from ambient pressure to 2.87 GPa. During the compression process, changes were observed in the behavior of the vibrational modes that raise suspicion of two possible conformational transitions around 0.67 GPa and 2.09 GPa. This work also presents an analysis of the vibrational modes as a function of temperature, where Raman spectroscopy measurements were performed in the range from 13 to 295 K. During the cooling process, changes were observed that suggest two possible phase transitions at 175 and 70 K. |
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Silva, Rômulo Sampaio daLima Júnior, José Alves de2022-02-25T16:50:14Z2022-02-25T16:50:14Z2022Silva, R. S. Espectroscopia Raman de cristais de DL-norleucina em altas pressões. 79 f. Dissertação (Mestrado em Física) - Centro de Ciências, Universidade Federal do Ceará, Fortaleza, 2022.http://www.repositorio.ufc.br/handle/riufc/64189Amino acids are the basic building blocks of proteins, which are indispensable for life. In the solid state, the stability of the structure is mainly maintained by hydrogen bonding that occurs between the nitrogen of the amino group and the oxygen of the carboxylic group. Mainly due to the versatility of their structures, amino acids can form polymorphic structures, bind to other amino acids forming dipeptides or even to other molecules and atoms such as: metals, organic and inorganic molecules, forming salts and metallics creating new materials with properties different from those of pure amino acids and even in some cases with potential technological applications mainly non-linear optical properties with potential applicability in electronic devices and pharmaceutical industry. Numerous works have been described in the study of the stability of the structure of amino acids both as a function of pressure and temperature. Several phase transitions have been reported. In this work we present a study by Raman spectroscopy of the DL-norleucine crystal as a function of the hydrostatic pressure varying from ambient pressure to 2.87 GPa. During the compression process, changes were observed in the behavior of the vibrational modes that raise suspicion of two possible conformational transitions around 0.67 GPa and 2.09 GPa. This work also presents an analysis of the vibrational modes as a function of temperature, where Raman spectroscopy measurements were performed in the range from 13 to 295 K. During the cooling process, changes were observed that suggest two possible phase transitions at 175 and 70 K.Os aminoácidos são as unidades básicas formadoras das proteínas, que são indispensáveis para a vida. No estado sólido a estabilidade da estrutura dos aminoácidos é mantida principalmente por ligações de hidrogênio que ocorrem entre o nitrogênio do grupo amino e o oxigênio do grupo carboxílico. Graças, principalmente, à versatilidade de suas estruturas os aminoácidos podem formar estruturas polimórficas, se ligar a outros aminoácidos formando dipeptídeos ou ainda a outras moléculas e átomos como: metais, ácidos, moléculas orgânicas e inorgânicas, formando sais e complexos metálicos, criando novos materiais com propriedades distintas dos aminoácidos puros e inclusive em alguns casos com potencial aplicações tecnológicas, principalmente propriedades de ótica não linear com potencial aplicabilidade em dispositivo eletrônicos e indústria farmacêutica. Inúmeros trabalhos têm sido publicados reportando o estudo da estabilidade da estrutura dos aminoácidos, tanto em função da pressão quanto da temperatura. Diversas transições de fase têm sido reportadas. Neste trabalho apresentamos um estudo por espectroscopia Raman do cristal de DL-norleucina em função da pressão hidrostática variando desde a pressão ambiente até 2,87 GPa. Durante o processo de compressão, foram observadas modificações no comportamento dos modos vibracionais que levantam suspeitas de duas possíveis transições conformacionais por volta de 0,67 GPa e 2,09 GPa. Este trabalho também apresenta uma análise dos modos vibracionais em função da temperatura, onde medidas de espectroscopia Raman foram realizadas no intervalo de 13 a 295 K. Durante o processo de resfriamento, foram verificadas alterações que sugerem duas possíveis transições de fase em 175 e 70 K.AminoácidosNorleucinaEspectroscopia RamanAltas pressõesBaixas temperaturasEspectroscopia Raman de cristais de DL-norleucina em altas pressõesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisporreponame:Repositório Institucional da Universidade Federal do Ceará (UFC)instname:Universidade Federal do Ceará (UFC)instacron:UFCinfo:eu-repo/semantics/openAccessLICENSElicense.txtlicense.txttext/plain; charset=utf-82158http://repositorio.ufc.br/bitstream/riufc/64189/4/license.txte63c6ed4faa81e8b90d2fac75971a7d6MD54ORIGINAL2022_dis_rssilva.pdf2022_dis_rssilva.pdfapplication/pdf5404039http://repositorio.ufc.br/bitstream/riufc/64189/5/2022_dis_rssilva.pdf7fdd7ce54c521cf758c0d75ef5b526a3MD55riufc/641892022-11-21 11:17:46.698oai:repositorio.ufc.br:riufc/64189TElDRU7Dh0EgREUgQVJNQVpFTkFNRU5UTyBFIERJU1RSSUJVScOHw4NPIE7Dg08tRVhDTFVTSVZBIA0KDQpBbyBjb25jb3JkYXIgY29tIGVzdGEgbGljZW7Dp2EsIHZvY8OqKHMpIGF1dG9yKGVzKSBvdSB0aXR1bGFyKGVzKSBkb3MgZGlyZWl0b3MgYXV0b3JhaXMgZGEgb2JyYSBhcXVpIGRlc2NyaXRhIGNvbmNlZGUobSkgw6AgVW5pdmVyc2lkYWRlIEZlZGVyYWwgZG8gQ2VhcsOhLCBnZXN0b3JhIGRvIFJlcG9zaXTDs3JpbyBJbnN0aXR1Y2lvbmFsIGRhIFVGQyAtIFJJL1VGQywgbyBkaXJlaXRvIG7Do28tZXhjbHVzaXZvIGRlIHJlcHJvZHV6aXIsIGNvbnZlcnRlciAoY29tbyBkZWZpbmlkbyBhYmFpeG8pIGUvb3UgZGlzdHJpYnVpciBvIGRvY3VtZW50byBkZXBvc2l0YWRvIGVtIGZvcm1hdG8gaW1wcmVzc28sIGVsZXRyw7RuaWNvIG91IGVtIHF1YWxxdWVyIG91dHJvIG1laW8uIFZvY8OqIGNvbmNvcmRhKG0pIHF1ZSBhIFVuaXZlcnNpZGFkZSBGZWRlcmFsIGRvIENlYXLDoSwgZ2VzdG9yYSBkbyBSZXBvc2l0w7NyaW8gSW5zdGl0dWNpb25hbCBkYSBVRkMgLSBSSS9VRkMsIHBvZGUsIHNlbSBhbHRlcmFyIG8gY29udGXDumRvLCBjb252ZXJ0ZXIgbyBhcnF1aXZvIGRlcG9zaXRhZG8gYSBxdWFscXVlciBtZWlvIG91IGZvcm1hdG8gY29tIGZpbnMgZGUgcHJlc2VydmHDp8Ojby4gVm9jw6oocykgdGFtYsOpbSBjb25jb3JkYShtKSBxdWUgYSBVbml2ZXJzaWRhZGUgRmVkZXJhbCBkbyBDZWFyw6EsIGdlc3RvcmEgZG8gUmVwb3NpdMOzcmlvIEluc3RpdHVjaW9uYWwgZGEgVUZDIC0gUkkvVUZDLCBwb2RlIG1hbnRlciBtYWlzIGRlIHVtYSBjw7NwaWEgZGVzdGUgZGVww7NzaXRvIHBhcmEgZmlucyBkZSBzZWd1cmFuw6dhLCBiYWNrLXVwIGUvb3UgcHJlc2VydmHDp8Ojby4gVm9jw6ogZGVjbGFyYSBxdWUgYSBhcHJlc2VudGHDp8OjbyBkbyBzZXUgdHJhYmFsaG8gw6kgb3JpZ2luYWwgZSBxdWUgdm9jw6oocykgcG9kZShtKSBjb25jZWRlciBvcyBkaXJlaXRvcyBjb250aWRvcyBuZXN0YSBsaWNlbsOnYS4gVm9jw6ogdGFtYsOpbSBkZWNsYXJhKG0pIHF1ZSBvIGVudmlvIMOpIGRlIHNldSBjb25oZWNpbWVudG8gZSBuw6NvIGluZnJpbmdlIG9zIGRpcmVpdG9zIGF1dG9yYWlzIGRlIG91dHJhIHBlc3NvYSBvdSBpbnN0aXR1acOnw6NvLiBDYXNvIG8gZG9jdW1lbnRvIGEgc2VyIGRlcG9zaXRhZG8gY29udGVuaGEgbWF0ZXJpYWwgcGFyYSBvIHF1YWwgdm9jw6oocykgbsOjbyBkZXTDqW0gYSB0aXR1bGFyaWRhZGUgZG9zIGRpcmVpdG9zIGRlIGF1dG9yYWlzLCB2b2PDqihzKSBkZWNsYXJhKG0pIHF1ZSBvYnRldmUgYSBwZXJtaXNzw6NvIGlycmVzdHJpdGEgZG8gdGl0dWxhciBkb3MgZGlyZWl0b3MgYXV0b3JhaXMgZGUgY29uY2VkZXIgw6AgVW5pdmVyc2lkYWRlIEZlZGVyYWwgZG8gQ2VhcsOhLCBnZXN0b3JhIGRvIFJlcG9zaXTDs3JpbyBJbnN0aXR1Y2lvbmFsIGRhIFVGQyAtIFJJL1VGQywgb3MgZGlyZWl0b3MgcmVxdWVyaWRvcyBwb3IgZXN0YSBsaWNlbsOnYSBlIHF1ZSBvcyBtYXRlcmlhaXMgZGUgcHJvcHJpZWRhZGUgZGUgdGVyY2Vpcm9zLCBlc3TDo28gZGV2aWRhbWVudGUgaWRlbnRpZmljYWRvcyBlIHJlY29uaGVjaWRvcyBubyB0ZXh0byBvdSBjb250ZcO6ZG8gZGEgYXByZXNlbnRhw6fDo28uDQogQ0FTTyBPIFRSQUJBTEhPIERFUE9TSVRBRE8gVEVOSEEgU0lETyBGSU5BTkNJQURPIE9VIEFQT0lBRE8gUE9SIFVNIMOTUkfDg08sIFFVRSBOw4NPIEEgSU5TVElUVUnDh8ODTyBERVNURSBSRVBPU0lUw5NSSU86IFZPQ8OKIERFQ0xBUkEgVEVSIENVTVBSSURPIFRPRE9TIE9TIERJUkVJVE9TIERFIFJFVklTw4NPIEUgUVVBSVNRVUVSIE9VVFJBUyBPQlJJR0HDh8OVRVMgUkVRVUVSSURBUyBQRUxPIENPTlRSQVRPIE9VIEFDT1JETy4gDQpPIHJlcG9zaXTDs3JpbyBpZGVudGlmaWNhcsOhIGNsYXJhbWVudGUgbyBzZXUocykgbm9tZShzKSBjb21vIGF1dG9yKGVzKSBvdSB0aXR1bGFyKGVzKSBkbyBkaXJlaXRvIGRlIGF1dG9yKGVzKSBkbyBkb2N1bWVudG8gc3VibWV0aWRvIGUgZGVjbGFyYSBxdWUgbsOjbyBmYXLDoSBxdWFscXVlciBhbHRlcmHDp8OjbyBhbMOpbSBkYXMgcGVybWl0aWRhcyBwb3IgZXN0YSBsaWNlbsOnYS4NClJlcG9zaXTDs3JpbyBJbnN0aXR1Y2lvbmFsIGRhIFVGQy4NCg==Repositório InstitucionalPUBhttp://www.repositorio.ufc.br/ri-oai/requestbu@ufc.br || repositorio@ufc.bropendoar:2022-11-21T14:17:46Repositório Institucional da Universidade Federal do Ceará (UFC) - Universidade Federal do Ceará (UFC)false |
| dc.title.pt_BR.fl_str_mv |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| title |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| spellingShingle |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões Silva, Rômulo Sampaio da Aminoácidos Norleucina Espectroscopia Raman Altas pressões Baixas temperaturas |
| title_short |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| title_full |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| title_fullStr |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| title_full_unstemmed |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| title_sort |
Espectroscopia Raman de cristais de DL-norleucina em altas pressões |
| author |
Silva, Rômulo Sampaio da |
| author_facet |
Silva, Rômulo Sampaio da |
| author_role |
author |
| dc.contributor.author.fl_str_mv |
Silva, Rômulo Sampaio da |
| dc.contributor.advisor1.fl_str_mv |
Lima Júnior, José Alves de |
| contributor_str_mv |
Lima Júnior, José Alves de |
| dc.subject.por.fl_str_mv |
Aminoácidos Norleucina Espectroscopia Raman Altas pressões Baixas temperaturas |
| topic |
Aminoácidos Norleucina Espectroscopia Raman Altas pressões Baixas temperaturas |
| description |
Amino acids are the basic building blocks of proteins, which are indispensable for life. In the solid state, the stability of the structure is mainly maintained by hydrogen bonding that occurs between the nitrogen of the amino group and the oxygen of the carboxylic group. Mainly due to the versatility of their structures, amino acids can form polymorphic structures, bind to other amino acids forming dipeptides or even to other molecules and atoms such as: metals, organic and inorganic molecules, forming salts and metallics creating new materials with properties different from those of pure amino acids and even in some cases with potential technological applications mainly non-linear optical properties with potential applicability in electronic devices and pharmaceutical industry. Numerous works have been described in the study of the stability of the structure of amino acids both as a function of pressure and temperature. Several phase transitions have been reported. In this work we present a study by Raman spectroscopy of the DL-norleucine crystal as a function of the hydrostatic pressure varying from ambient pressure to 2.87 GPa. During the compression process, changes were observed in the behavior of the vibrational modes that raise suspicion of two possible conformational transitions around 0.67 GPa and 2.09 GPa. This work also presents an analysis of the vibrational modes as a function of temperature, where Raman spectroscopy measurements were performed in the range from 13 to 295 K. During the cooling process, changes were observed that suggest two possible phase transitions at 175 and 70 K. |
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2022 |
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2022-02-25T16:50:14Z |
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2022-02-25T16:50:14Z |
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2022 |
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info:eu-repo/semantics/masterThesis |
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masterThesis |
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Silva, R. S. Espectroscopia Raman de cristais de DL-norleucina em altas pressões. 79 f. Dissertação (Mestrado em Física) - Centro de Ciências, Universidade Federal do Ceará, Fortaleza, 2022. |
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http://www.repositorio.ufc.br/handle/riufc/64189 |
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Silva, R. S. Espectroscopia Raman de cristais de DL-norleucina em altas pressões. 79 f. Dissertação (Mestrado em Física) - Centro de Ciências, Universidade Federal do Ceará, Fortaleza, 2022. |
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