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	Provedor de dados BJMBR (2) ArchiMer (1) Braz. J. Plant Physiol. (1) Autor Almeida Filho,Humberto A (1) Araujo,P.S. de (1) Bloch Jr,Carlos (1) Calderon,Leonardo A (1) Costa,M.H.B. (1) Faljoni-Alário,A. (1) Freitas,Sonia M (1) Günther,A.R. (1) Hugall, Andrew F (1) Medrano,Francisco J (1) O’hara, Timothy D (1) Quintilio,W. (1) Rogana,E. (1) Sant'Anna,O.A. (1) Santoro,M.M. (1) Santoro,Marcelo M (1) Teles,Rozeni C. L (1) Weber, Alexandra At (1) Mais... Palavra-chave Protein stability (4) Adjuvant (1) Drug delivery system (1) Echinodermata (1) Hydrophobic modification (1) Inga cylindrica [Vell.] Mart (1) Leguminosae (1) Mimosoideae (1) Positive selection (1) Pressure adaptation (1) Protease inhibitor (1) Protein folding (1) Protein pH titration (1) SS-trypsin (1) TC P-1 (1) Trypsin inhibitor (1) Vaccine delivery system (1) Mais... Tipo do documento Info:eu-repo/semantics/article (2) Info:eu-repo/semantics/other (1) Text (1) Ano 2020 (1) 2010 (1) 2002 (1) 1997 (1) País Brazil (3) France (1) Idioma Inglês (4)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última The use of protein structure/activity relationships in the rational design of stable particulate delivery systems BJMBR Costa,M.H.B.; Quintilio,W.; Sant'Anna,O.A.; Faljoni-Alário,A.; Araujo,P.S. de. The recombinant heat shock protein (18 kDa-hsp) from Mycobacterium leprae was studied as a T-epitope model for vaccine development. We present a structural analysis of the stability of recombinant 18 kDa-hsp during different processing steps. Circular dichroism and ELISA were used to monitor protein structure after thermal stress, lyophilization and chemical modification. We observed that the 18 kDa-hsp is extremely resistant to a wide range of temperatures (60% of activity is retained at 80ºC for 20 min). N-Acylation increased its ordered structure by 4% and decreased its ß-T1 structure by 2%. ELISA demonstrated that the native conformation of the 18 kDa-hsp was preserved after hydrophobic modification by acylation. The recombinant 18 kDa-hsp resists to a... Tipo: Info:eu-repo/semantics/other Palavras-chave: Protein stability; Hydrophobic modification; Vaccine delivery system; Drug delivery system; Adjuvant. Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2002000600014 pH titration of native and unfolded ß-trypsin: evaluation of the D D G0 titration and the carboxyl pK values BJMBR Günther,A.R.; Santoro,M.M.; Rogana,E.. The stabilizing free energy of ß-trypsin was determined by hydrogen ion titration. In the pH range from 3.0 to 7.0, the change in free energy difference for the stabilization of the native protein relative to the unfolded one (<!-- $MVD$:face("Symbol") -->D D G0 titration) was 9.51 ± 0.06 kcal/mol. An isoelectric point of 10.0 was determined, allowing us to calculate the Tanford and Kirkwood electrostatic factor w. This factor presented a nonlinear behavior and indicated more than one type of titratable carboxyl groups in ß-trypsin. In fact, one class of carboxyl group with a pK = 3.91 ± 0.01 and another one with a pK = 4.63 ± 0.03 were also found by hydrogen ion titration of the protein in the folded state Tipo: Info:eu-repo/semantics/article Palavras-chave: SS-trypsin; Protein stability; Protein pH titration. Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997001100003 Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds Braz. J. Plant Physiol. Calderon,Leonardo A; Almeida Filho,Humberto A; Teles,Rozeni C. L; Medrano,Francisco J; Bloch Jr,Carlos; Santoro,Marcelo M; Freitas,Sonia M. Inga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds. ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM). Circular dichroism analysis revealed that this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors. ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by Tm of 70.0 ºC and ΔG25 of 48.5 ± 0.7 kJ.mol-1. The values of ΔG25 at pH 1.6 (22.5 ± 1.2 kJ.mol-1) and pH 10.0 (31.5 ± 1.0... Tipo: Info:eu-repo/semantics/article Palavras-chave: Inga cylindrica [Vell.] Mart; Leguminosae; Mimosoideae; Protease inhibitor; Protein stability; Trypsin inhibitor. Ano: 2010 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202010000200001 Convergent Evolution and Structural Adaptation to the Deep Ocean in the Protein-Folding Chaperonin CCTα ArchiMer Weber, Alexandra At; Hugall, Andrew F; O’hara, Timothy D. The deep ocean is the largest biome on Earth and yet it is among the least studied environments of our planet. Life at great depths requires several specific adaptations; however, their molecular mechanisms remain understudied. We examined patterns of positive selection in 416 genes from four brittle star (Ophiuroidea) families displaying replicated events of deep-sea colonization (288 individuals from 216 species). We found consistent signatures of molecular convergence in functions related to protein biogenesis, including protein folding and translation. Five genes were recurrently positively selected, including chaperonin-containing TCP-1 subunit α (CCTα), which is essential for protein folding. Molecular convergence was detected at the functional and... Tipo: Text Palavras-chave: Echinodermata; TC P-1; Protein folding; Positive selection; Protein stability; Pressure adaptation. Ano: 2020 URL: https://archimer.ifremer.fr/doc/00659/77136/78452.pdf Registros recuperados: 4 Primeira ... 1 ... Última

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