Conformation of an octapeptide fragment (2-9) of kaliocin-1 in DMSO-d6 by 1H NMR and restrained molecular dynamics.
Indian J Biochem Biophys
;
2007 Feb; 44(1): 44-9
Artigo
em Inglês
| IMSEAR
| ID: sea-27422
ABSTRACT
Kaliocin-1, a 31-residue synthetic peptide (FFSASCVPGADKGQFPNLCRLCA GTGENKCA), which has shown the antimicrobial activity forms the 152-182 fragment of human lactoferrin (HLf). As the octapeptide FSASCVPG forms the 2-9 fragment of kaliocin-1, in the present study, its conformation in dimethyl sulfoxide-d6 (DMSO-d6) has been determined using two-dimensional (2D) nuclear magnetic resonance (NMR) spectroscopy as well as restrained molecular dynamics. Sequence specific assignments of all the 1H resonances have been carried out using 2D correlation experiments (2D DQF-COSY, TOCSY and ROESY). In dimethyl sulfoxide-d6 at 25 degrees C, the octapeptide adopts a predominantly extended backbone conformation. The calculated structure resembles closely with the reported structure of the corresponding fragment of HLf. The peptide also has sequence and structural similarity with the corresponding fragments of lactoferrins from other organisms.
Texto completo:
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Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Fragmentos de Peptídeos
/
Termodinâmica
/
Humanos
/
Dados de Sequência Molecular
/
Proteínas de Transporte
/
Modelos Moleculares
/
Sequência de Aminoácidos
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Estrutura Secundária de Proteína
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Ressonância Magnética Nuclear Biomolecular
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
2007
Tipo de documento:
Artigo
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