scholarly journals Determination of the Solution-Bound Conformation of an Amino Acid Binding Protein by NMR Paramagnetic Relaxation Enhancement: Use of a Single Flexible Paramagnetic Probe with Improved Estimation of Its Sampling Space

2009 ◽  
Vol 131 (27) ◽  
pp. 9532-9537 ◽  
Author(s):  
Guillermo A. Bermejo ◽  
Marie-Paule Strub ◽  
Chien Ho ◽  
Nico Tjandra
Keyword(s):  
Amino Acid ◽  
Binding Protein ◽  
Paramagnetic Relaxation ◽  
Paramagnetic Relaxation Enhancement ◽  
Acid Binding Protein ◽  
Paramagnetic Probe ◽  
Solution Bound ◽  
Amino Acid Binding

scholarly journals Biophysical insights into a highly selective L-arginine-binding lipoprotein of a pathogenic treponeme

2018 ◽  
Author(s):  
Ranjit K. Deka ◽  
Wei Z. Liu ◽  
Shih-Chia Tso ◽  
Michael V. Norgard ◽  
Chad A. Brautigam
Keyword(s):  
Amino Acid ◽  
Single Molecule ◽  
Binding Protein ◽  
Treponema Pallidum ◽  
Titration Calorimetry ◽  
Biophysical Studies ◽  
Differential Scanning Fluorimetry ◽  
Periplasmic Proteins ◽  
Amino Acid Binding

ABSTRACTBiophysical and biochemical studies on the lipoproteins and other periplasmic proteins from the spirochetal speciesTreponema pallidumhave yielded numerous insights into the functioning of the organism’s peculiar membrane organization, its nutritional requirements, and intermediary metabolism. However, not allT. pallidumproteins have proven to be amenable to biophysical studies. One such recalcitrant protein is Tp0309, a putative polar-amino-acid-binding protein of an ABC transporter system. To gain further information on its possible function, a homolog of the protein from the related speciesT. vincentiiwas used as a surrogate. This protein, Tv2483, was crystallized, resulting in the determination of its crystal structure at a resolution of 1.75 Å. The protein has a typical fold for a ligand-binding protein, and a single molecule of L-arginine was bound between its two lobes. Differential scanning fluorimetry and isothermal titration calorimetry experiments confirmed that L-arginine bound to the protein with unusually high selectivity. However, further comparison to Tp0309 showed differences in key amino-acid-binding residues may impart an alternate specificity for theT. pallidumprotein.

Revision of the amino acid sequence of human heart fatty acid-binding protein

1990 ◽  
pp. 127-133
Author(s):  
Torsten Börchers ◽  
Peter Højrup ◽  
Søren U. Nielsen ◽  
Peter Roepstorff ◽  
Friedrich Spener ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Heart ◽  
Fatty Acid Binding Protein ◽  
Binding Protein ◽  
Fatty Acid Binding ◽  
Acid Binding Protein

A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form

Development ◽  
1999 ◽  
Vol 126 (18) ◽  
pp. 4077-4086 ◽  
Author(s):  
W. Hampe ◽  
J. Urny ◽  
I. Franke ◽  
S.A. Hoffmeister-Ullerich ◽  
D. Herrmann ◽  
...  
Keyword(s):  
Stem Cells ◽  
Amino Acid ◽  
Transmembrane Domain ◽  
Binding Protein ◽  
Amino Acid Sequences ◽  
Secreted Protein ◽  
Specific Antibodies ◽  
Head Activator ◽  
Carboxy Terminal

The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.

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