Molecular dynamics and ion mobility spectrometry study of model ß-hairpin peptide, trpzip1.
J Phys Chem A
; 115(17): 4427-35, 2011 May 05.
Article
em En
| MEDLINE
| ID: mdl-21476523
ABSTRACT
Here, we explore the conformations of gas phase, protonated tryptophan zipper 1 (trpzip1) ions and its six derivatives by an enhanced sampling molecular dynamics, specially the integrated tempering sampling molecular dynamics simulation (ITS-MDS). The structural distributions obtained from ITS-MDS are compared with results obtained from matrix-assisted laser desorption ionization (MALDI)-ion mobility-mass spectrometry (IM-MS). The IM-MS measured collision cross-section (CCS) profiles compare well with the calculated CCS profiles obtained from ITS-MDS. Although ß-turn structures are preferred for solution phase species, the ITS-MDS and IM-MS structural analysis suggests that the γ-turn structures are preferred for gas-phase, unsolvated trpzip1 [M + H](+) ions. In addition, the data suggests that the energy landscape of the gas phase peptide ions is sensitive to the site of protonation as well as intramolecular interactions involving the lysine side chain.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Triptofano
/
Simulação de Dinâmica Molecular
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article