Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR spectroscopy.
Eur J Biochem
; 251(3): 781-6, 1998 Feb 01.
Article
en En
| MEDLINE
| ID: mdl-9490052
Two- and three-dimensional heteronuclear NMR experiments have been performed to identify internally bound water molecules in the solution structure of bovine heart fatty-acid-binding protein (heart FABP). NOE and rotating-frame NOE (ROE) cross peaks between protein protons and protons of bound water molecules were observed in two-dimensional H2O-ROE/NOE-1H,15N-heteronuclear single quantum coherence spectra recorded from a uniformly 13C/15N-enriched sample of bovine heart FABP. Contacts between water protons and 23 NH protons of the protein backbone were identified. The protein structure consists of 10 antiparallel beta-strands (betaA-betaJ), forming two nearly orthogonal beta-sheets, and a short helix-turn-helix motif connecting beta-strands A and B. The spatial folding resembles a beta-barrel. Most of the water molecules are localized in the gap between beta-strands D and E, and near the two alpha-helices. In the delipidated heart FABP additional contacts between water molecules and NH protons could be observed using a three-dimensional rotating frame Overhauser 1H,15N heteronuclear single quantum coherence experiment obtained with a 15N-labeled sample of apo-heart FABP.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Apoproteínas
/
Proteínas Portadoras
/
Estructura Secundaria de Proteína
/
Proteína P2 de Mielina
/
Miocardio
/
Proteínas de Neoplasias
Límite:
Animals
Idioma:
En
Revista:
Eur J Biochem
Año:
1998
Tipo del documento:
Article
País de afiliación:
Alemania
Pais de publicación:
Reino Unido