Data/hora: 21/06/2024 15:52:22

Biblioteca(s): | Embrapa Instrumentação.
Data corrente: | 22/12/1999
Data da última atualização: | 02/03/2010
Autoria: | NASCIMENTO, O. R.; MARTIN-NETO, L.; TABAK, M.; WAJJNBERG, E.; BEMSKI, G.; WINKLER, H.; BILL, E.; TRAUTWEIN, A. X.
Afiliação: | USP-IFSC; EMBRAPA-CNPDIA.
Título: | Equilibrium of conformational states in met-myoglobin molecules as a function of dehydration level: an EPR and Mossbauer studies.
Ano de publicação: | 1992
Fonte/Imprenta: | In: ENCONTRO NACIONAL DE FISICA DA MATERIA CONDENSADA, 15., maio 1992, Caxambu, MG. Programa e resumos... Sao Paulo: Sociedade Brasileira de Fisica, 1992.
Páginas: | p.59.
Idioma: | Inglês
Conteúdo: | Protein have been shown to be dynamics molecules and exist in several conformational states and substates. The equilibrium between these conformations depends of different factors and has an important role in biological behavior. In this work the role of hydration degree is investigated in the spin and valence equilibria of the iron reaction center of the met-myoglobin from sperm whale and horse muscles. Our results show the lost of EPR paramagnetism of these molecules in low hydration suggesting valence changes from ferric to ferrous state as well as high to low spin states of the ferric forms. These results are quantified in terms of different paramagnetic species by double integration of the EPR spectra corrected by g values and population effect due zero field splitting and temperature. Mossbauer measurements were taken with the samples in different degree of hydration, pure and reacted with NO nitric oxide gas. Interpretation of these Mossbauer spectra is in progress.
Palavras-Chave: | Dehydration; EPR; Met-myoglobin; Molecules; Mossbauer.
Categoria do assunto: | --
Registro original: | Embrapa Instrumentação (CNPDIA)
Exemplares: | CNPDIA - (5291-1) - UPC - SP - -- - PROCI-92.00037 -  - 1992.00037 - DIS