Related ArticlesDetermination of the secondary structural elements of chicken liver fatty acid binding protein by two-dimensional homonuclear NMR.
Biopolymers. 1999 Jul;50(1):1-11
Authors: Schievano E, Mammi S, Peggion E
A conformational study in solution of the fatty acid binding protein from chicken liver is presented. The nearly complete sequence-specific 1H resonance assignment was achieved from homonuclear two-dimensional nmr experiments using a sample of native protein. The principal elements of secondary structure were identified: 10 antiparallel beta-strands and one helical segment followed by a turn comprising 5 residues. These elements correspond closely with those of the crystal structure of the related protein, and two new secondary structural features obtained from the nmr data are the beta-sheet conformation between the first and the last beta-strand in the protein sequence, as well as a helical loop at the N-terminus of the polypeptide chain.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
An NMR-Based Structural Rationale for Contrasting Stoichiometry and Ligand Binding Site(s) in Fatty Acid-binding Proteins.
Biochemistry. 2011 Jan 12;
Authors: He Y, Estephan R, Yang X, Vela A, Wang H, Bernard C, Stark RE
Liver fatty acid-binding protein (LFABP) is a 14-kDa cytosolic polypeptide, differing from other family members in number of ligand binding sites, diversity of bound ligands, and transfer of fatty acid(s) to...
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[NMR paper] Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures
Fatty acid interactions with proteins: what X-ray crystal and NMR solution structures tell us.
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Prog Lipid Res. 2004 May;43(3):177-99
Authors: Hamilton JA
The interactions of fatty acids with proteins have been studied by a variety of conventional approaches for decades. However, only limited aspects of fatty acid-protein interactions have been elucidated, even with the integration of information gleaned from the many techniques....
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[NMR paper] NMR assignment and structural characterization of the fatty acid binding protein from
NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria.
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J Biomol NMR. 2003 Apr;25(4):355-6
Authors: Lücke C, Kizilbash N, van Moerkerk HT, Veerkamp JH, Hamilton JA
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[NMR paper] Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C
Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
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Biochemistry. 2001 Oct 23;40(42):12604-11
Authors: Beringhelli T, Goldoni L, Capaldi S, Bossi A, Perduca M, Monaco HL
Two different groups of liver fatty acid-binding proteins (L-FABPs) are known: the mammalian type and the basic type. Very few members of this second group of L-FABPs have been...
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[NMR paper] Sequential assignments and identification of secondary structure elements of the coli
Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMR.
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Biochemistry. 1994 Oct 18;33(41):12347-55
Authors: Osborne MJ, Lian LY, Wallis R, Reilly A, James R, Kleanthous C, Moore GR
1H-1H, 1H-15N, and 1H-1H-15N multidimensional NMR spectroscopic studies of the 86 amino...
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[NMR paper] Proton NMR sequence-specific assignments and secondary structure of a receptor bindin
Proton NMR sequence-specific assignments and secondary structure of a receptor binding domain of mouse gamma-interferon.
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Biochemistry. 1993 Jun 1;32(21):5650-5
Authors: Sakai TT, Jablonsky MJ, DeMuth PA, Krishna NR, Jarpe MA, Johnson HM
Previous studies using synthetic peptides and monoclonal antibodies have implicated the N-terminal 39-residue segment as a receptor binding region of mouse gamma-interferon...
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[NMR paper] 1H NMR sequential assignments and identification of secondary structural elements in
1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas.
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Biochemistry. 1992 Feb 25;31(7):1961-8
Authors: Ye XM, Pochapsky TC, Pochapsky SS
Sequential 1H resonance assignments and secondary structural features of putidaredoxin (Pdx), a 106-residue globular protein consisting of...
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[NMR paper] 13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty ac
13C NMR studies of fatty acid-protein interactions: comparison of homologous fatty acid-binding proteins produced in the intestinal epithelium.
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Mol Cell Biochem. 1990 Oct 15-Nov 8;98(1-2):101-10
Authors: Cistola DP, Sacchettini JC, Gordon JI
A high-resolution, solution-state NMR method for characterizing and comparing the interactions between carboxyl 13C-enriched fatty acids (FA) and...
Determination of the secondary structural elements of chicken liver fatty acid bindin
Linear Mode
