Abstract

The function of this core unit is to centralize the facilities and expertise of the major physico-chemical techniques utilized in the project areas forming the Program Project. FACILITIES PROVIDED BY THE CORE UNIT 1) X-ray Scattering/Diffraction/Crystallography 2) Nuclear Magnetic Resonance Spectroscopy Nuclei: 13/C, 1/H, 2/H, 31/P, 15/N and all other NMR nuclei 3) Calorimetry Standard and high sensitivity adiabatic differential scanning, titration 4) Electron Microscopy Negative staining, sectioning and morphological analysis 5) Structural Electron Microscopy and Image Processing 6) Protein Crystallization 7) Circular Dichroic Spectroscopy Near and far UV 8) Molecular Modeling, Graphics, Energy Minimization and Molecular Dynamics 9) Crystallographic Computing 10) Surface Monolayer Techniques

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Program Projects (P01)
Project #
5P01HL026335-20
Application #
6302139
Study Section
Project Start
2000-01-01
Project End
2000-12-31
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
2000
Total Cost
$346,980
Indirect Cost

  Institution

Name
Boston University
Department
Type
DUNS #
604483045
City
Boston
State
MA
Country
United States
Zip Code
02118

  Publications

Melchior, John T; Walker, Ryan G; Cooke, Allison L et al. (2017) A consensus model of human apolipoprotein A-I in its monomeric and lipid-free state. Nat Struct Mol Biol 24:1093-1099
Gursky, Olga (2015) Structural stability and functional remodeling of high-density lipoproteins. FEBS Lett 589:2627-39
Mei, Xiaohu; Atkinson, David (2015) Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development. Arch Med Res 46:351-60
Wang, Libo; Mei, Xiaohu; Atkinson, David et al. (2014) Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces. J Lipid Res 55:478-92
Gorshkova, Irina N; Mei, Xiaohu; Atkinson, David (2014) Binding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia. J Lipid Res 55:1876-85
Mitsche, Matthew A; Packer, Laura E; Brown, Jeffrey W et al. (2014) Surface tensiometry of apolipoprotein B domains at lipid interfaces suggests a new model for the initial steps in triglyceride-rich lipoprotein assembly. J Biol Chem 289:9000-12
Gursky, Olga (2013) Crystal structure of ?(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt buckle, double hairpin and trefoil/tetrafoil. J Mol Biol 425:1-16
Khachfe, Hassan M; Atkinson, David (2013) Conformation and stability properties of B17: II. Analytical investigations using differential scanning calorimetry. Eur Biophys J 42:309-14
Mitsche, Matthew A; Small, Donald M (2013) Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic ?-helices. J Lipid Res 54:1578-88
Meyers, Nathan L; Wang, Libo; Small, Donald M (2012) Apolipoprotein C-I binds more strongly to phospholipid/triolein/water than triolein/water interfaces: a possible model for inhibiting cholesterol ester transfer protein activity and triacylglycerol-rich lipoprotein uptake. Biochemistry 51:1238-48

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