Synchrotron radiation circular dichroism to study the binding of the DGAT1 peptides with substrates (2012)
- Authors:
- USP affiliated authors: BELTRAMINI, LEILA MARIA - IFSC ; ARAUJO, ANA PAULA ULIAN DE - IFSC
- Unidade: IFSC
- Subjects: ENZIMAS (ESTUDO); PROTEÍNAS; MEMBRANAS (BIOLOGIA)
- Language: Inglês
- Imprenta:
- Publisher: Wiley-Blackwell
- Publisher place: Oxford
- Date published: 2012
- Source:
- Título: FEBS Journal
- ISSN: 1742-464X
- Volume/Número/Paginação/Ano: v. 279, suppl. 1, p. 421, abstr. P 20-46, Sept. 2012
- Conference titles: Congress of the International Union of Biochemistry and Molecular Biology - IUBMB
-
ABNT
LOPES, J. L. S. et al. Synchrotron radiation circular dichroism to study the binding of the DGAT1 peptides with substrates. FEBS Journal. Oxford: Wiley-Blackwell. . Acesso em: 29 dez. 2025. , 2012 -
APA
Lopes, J. L. S., Beltramini, L. M., Wallace, B. A., & Araújo, A. P. U. de. (2012). Synchrotron radiation circular dichroism to study the binding of the DGAT1 peptides with substrates. FEBS Journal. Oxford: Wiley-Blackwell. -
NLM
Lopes JLS, Beltramini LM, Wallace BA, Araújo APU de. Synchrotron radiation circular dichroism to study the binding of the DGAT1 peptides with substrates. FEBS Journal. 2012 ; 279 421.[citado 2025 dez. 29 ] -
Vancouver
Lopes JLS, Beltramini LM, Wallace BA, Araújo APU de. Synchrotron radiation circular dichroism to study the binding of the DGAT1 peptides with substrates. FEBS Journal. 2012 ; 279 421.[citado 2025 dez. 29 ] - Pulchellin, a highly toxic type 2 ribosome-inactivating protein from Abrus pulchellus cloning: heterologous expression of A-chain and structural studies
- Heterologous expression, characterization and structural studies of a highly hydrophobic peptide from the HIV-1 capsid protein (P24)
- Deconstructing the DGAT1 enzyme: binding sites and substrate interactions
- Influence of the his tag on the structure of recombinant chlorocatechol 1,2-dioxygenase monitored by Circular Dichroism (CD) and assay activity
- Expression, purification and structural characterization of calflagin: a flagellar calcium-binding protein of Trypanosoma cruzi
- Expression, purification and structural characterization of F29: a flagellar calcium-binding protein of Trypanosoma cruzi
- Calflagin: stability and structural studies monitored by CD and fluoresecence
- Investigation of the bovine DGAT1 enzyme binding sites specificity
- Use of peptides to investigate the binding sites of the diacylglycerol acyltransferase1 enzyme
- Deconstructing the DGAT1 enzyme: membrane interactions at substrate binding sites
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
