[NMR paper] NMR and Docking Calculations Reveal Novel Atomistic Selectivity of a Synthetic High-Affinity Free Fatty Acid vs. Free Fatty Acids in Sudlow's Drug Binding Sites in Human Serum Albumin
NMR and Docking Calculations Reveal Novel Atomistic Selectivity of a Synthetic High-Affinity Free Fatty Acid vs. Free Fatty Acids in Sudlow's Drug Binding Sites in Human Serum Albumin
Saturation transfer difference (STD), inter-ligand NOEs (INPHARMA NMR), and docking calculations are reported for investigating specific binding sites of the high-affinity synthetic 7-nitrobenz-2-oxa-1,3-diazoyl-4-C(12) fatty acid (NBD-C(12) FA) with non-labeled human serum albumin (HSA) and in competition with the drugs warfarin and ibuprofen. A limited number of negative interligand NOEs between NBD-C(12)...
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12-27-2023 08:40 AM
[NMR paper] Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.
Biomol NMR Assign. 2019 Apr 02;:
Authors: Jones DNM, Wang J, Murphy EJ
...
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04-05-2019 08:33 AM
How Oliceridine (TRV-130) Binds and Stabilizes a ?-OpioidReceptor Conformational State That Selectively Triggers G ProteinSignaling Pathways
How Oliceridine (TRV-130) Binds and Stabilizes a ?-OpioidReceptor Conformational State That Selectively Triggers G ProteinSignaling Pathways
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00948/20161107/images/medium/bi-2016-00948x_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00948
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[NMR paper] Solution NMR studies of sterol carrier protein 2 like 2 (SCP2L2) reveal the insecticide specific structural characteristics of SCP2 proteins in Aedes Aegypti mosquitoes.
Solution NMR studies of sterol carrier protein 2 like 2 (SCP2L2) reveal the insecticide specific structural characteristics of SCP2 proteins in Aedes Aegypti mosquitoes.
Related Articles Solution NMR studies of sterol carrier protein 2 like 2 (SCP2L2) reveal the insecticide specific structural characteristics of SCP2 proteins in Aedes Aegypti mosquitoes.
Biochemistry. 2016 Aug 10;
Authors: Singarapu KK, Ahuja A, Potula PR, Ummanni R
Abstract
Sterol carrier protein 2 like 2 from Aedes aegypri (AeSCP2L2) plays an important role in...
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08-13-2016 02:13 AM
[NMR paper] Direct NMR Observation of Odorant Binding to Mouse Odorant Receptor MOR244-3.
Direct NMR Observation of Odorant Binding to Mouse Odorant Receptor MOR244-3.
Related Articles Direct NMR Observation of Odorant Binding to Mouse Odorant Receptor MOR244-3.
Anal Biochem. 2016 Mar 24;
Authors: Burger JL, Jeerage KM, Bruno TJ
Abstract
Mammals are able to perceive and differentiate a great number of structurally diverse odorants through the odorant's interaction with odorant receptors (ORs), proteins found within the cell membrane of olfactory sensory neurons. The natural gas industry has utilized human...
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03-29-2016 04:59 PM
[NMR paper] Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.
Sci Rep. 2013;3:2913
Authors: Ogura K, Okamura H
Abstract
Growth factor receptor-bound protein 2 (Grb2) is a small adapter protein composed of a single SH2 domain flanked by two SH3 domains. The...
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10-10-2013 09:38 PM
[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.
Related Articles Interaction of chicken liver basic fatty acid-binding protein with fatty acids: a 13C NMR and fluorescence study.
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...
Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail - Nature.com
Linear Mode
