[NMR paper] Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
J Biochem. 2013 Oct 4;
Authors: Yuasa N, Koyama T, Subedi GP, Yamaguchi Y, Matsushita M, Fujita-Yamaguchi Y
Abstract
T-antigen (Gal?1-3GalNAc?-1-Ser/Thr), also known as...
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[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):i
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Protein-ligand interactions are driven by many factors, including protein conformation and pH of the solution. Electrospray mass spectrometry can reveal the degree of protein folding from the distribution of...
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[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):895-903
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Human liver fatty acid binding protein (hL-FABP) is the most abundant cytosolic protein in the liver. This protein plays important roles associated to partitioning of fatty acids (FAs) to specific...
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
March 2012
Publication year: 2012
Source:Biochimie, Volume 94, Issue 3</br>
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The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to -6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition to regulating IGF actions, IGFBPs have IGF-independent functions. IGFBP-2, the largest member of this family, is over-expressed in many cancers and has been proposed as a possible target for the...
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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A rigid lanthanide binding tag for NMR structural analysis of carbohydrates.
A rigid lanthanide binding tag for NMR structural analysis of carbohydrates.
A rigid lanthanide binding tag for NMR structural analysis of carbohydrates.
Chem Commun (Camb). 2011 May 23;
Authors: Mallagaray A, Canales A, Domínguez G, Jiménez-Barbero J, Pérez-Castells J
The first synthesis of a carbohydrate molecule covalently bound to a rigid lanthanide binding tag is reported. This derivative has been designed as a new tool to provide long-range restraints for structural elucidation and molecular recognition studies of carbohydrates, thus...
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[NMR paper] NMR-based binding screen and structural analysis of the complex formed between alpha-
NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
Related Articles NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
J Biol Chem. 2002 Oct 4;277(40):37439-45
Authors: Zeng H, Hawrot E
The alpha18-mer...