Investigating the Conformational Transitions of Human Adipocyte Fatty Acid Binding Protein Upon Binding Leukotriene B4 by Solution-State NMR Spectroscopy
Investigating the Conformational Transitions of Human Adipocyte Fatty Acid Binding Protein Upon Binding Leukotriene B4 by Solution-State NMR Spectroscopy
Publication date: 2 February 2018 Source:Biophysical Journal, Volume 114, Issue 3, Supplement 1
Author(s): Kim N. Ha, Youlin Xia, Yenchi Tran, Gianluigi Veglia, David A. Bernlohr
[NMR paper] Structural determinants of ligand binding in the ternary complex of human ileal bile acid-binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR.
Structural determinants of ligand binding in the ternary complex of human ileal bile acid-binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR.
Related Articles Structural determinants of ligand binding in the ternary complex of human ileal bile acid-binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMR.
FEBS J. 2015 Nov 27;
Authors: Horváth G, Bencsura Á, Simon Á, Tochtrop GP, DeKoster GT, Covey DF, Cistola DP, Toke O
Abstract
Besides aiding digestion,...
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Investigating the Structural Dynamics Transitions of Human Adipocyte Fatty Acid Binding Protein by NMR Spectroscopy
Investigating the Structural Dynamics Transitions of Human Adipocyte Fatty Acid Binding Protein by NMR Spectroscopy
Publication date: 27 January 2015
Source:Biophysical Journal, Volume 108, Issue 2, Supplement 1</br>
Author(s): Kim N. Ha , Youlin Xia , Yenchi Tran , Adedolapo Ojoawo , Gianluigi Veglia , David A. Bernlohr</br>
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Structural Dynamics Studies of Fatty Acid Binding Protein-4 by Solution NMR Spectroscopy
Structural Dynamics Studies of Fatty Acid Binding Protein-4 by Solution NMR Spectroscopy
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Adedolapo Ojoawo , Choua Xiong , Kim N. Ha</br>
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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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[NMR paper] Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein
Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange.
Biochemistry. 1997 Feb 25;36(8):2278-90
Authors: Hodsdon ME, Cistola DP
The backbone dynamics of the liganded (holo) and unliganded (apo) forms of Escherichia...
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[NMR paper] The NMR solution structure of intestinal fatty acid-binding protein complexed with pa
The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: application of a novel distance geometry algorithm.
J Mol Biol. 1996 Dec 6;264(3):585-602
Authors: Hodsdon ME, Ponder JW, Cistola DP
The three-dimensional solution structure of rat...
Investigating the Conformational Transitions of Human Adipocyte Fatty Acid Binding Protein Upon Binding Leukotriene B4 by Solution-State NMR Spectroscopy
Linear Mode
