Journal Title
Title of Journal: Biomol NMR Assign
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Abbravation: Biomolecular NMR Assignments
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Publisher
Springer Netherlands
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Authors: Yunhuang Yang David Hoyt Jianjun Wang
Publish Date: 2007/07/28
Volume: 1, Issue: 1, Pages: 109-111
Abstract
ApoAI is the major protein component of the highdensity lipoprotein HDL that has been a hot subject of interests because of its antiatherogenic properties Lipidfree apoAI specifically binds to phospholipids triggering HDL formation Here we report a complete backbone assignment and nearly complete sidechain assignment of a Cterminal 24residue truncation mutant of mouse apoAI apoAI1216 in its lipidfree formThis work was supported by grants from a NIH RO1 grant HL076620 to JW and an International HDL Research Award to JW Part of the NMR experiments described in this manuscript were performed at the W R Wiley Environmental Molecular Sciences Laboratory a national scientific user facility sponsored by the US Department of Energy’s Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory PNNL PNNL is operated for the Department of Energy by Battelle
Keywords:
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Other Papers In This Journal:
- Letter to the Editor: Resonance assignment of SlyD from E. coli
- NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1
- 1 H, 13 C, 15 N resonance assignment of the chitin-binding protein CBP21 from Serratia marcescens
- Backbone nuclear magnetic resonance assignment of human deoxyuridine 5′-triphosphate nucleotidohydrolase (dUTPase)
- 1 H, 13 C, and 15 N assignment of the muscular LIM protein MLP/CRP3
- Backbone and sidechain 1 H, 13 C and 15 N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid
- 1 H, 13 C and 15 N assignment of the C-terminal domain of GNA2132 from Neisseria meningitidis
- 1 H, 13 C, 15 N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the Hv GR-RBP1 protein involved in the regulation of barley ( Hordeum vulgare L.) senescence
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