Abstract

The function of this core unit is to centralize the facilities and expertise of the major physical chemical and structural techniques utilized in the four project areas forming the Program Project. Facilities Provided by the Core Unit: 1) X-Ray Crystallography 2) Nuclear Magnetic Resonance Spectroscopy Nuclei: 13C, 1H, 2H, 31P, 15N and all other NMR nuclei 3) Calorimetry 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 Dichroism Spectroscopy Near and far UV 8) Molecular Modeling, Graphics, 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 #
5P01HL026335-30
Application #
8051585
Study Section
Heart, Lung, and Blood Initial Review Group (HLBP)
Project Start
Project End
Budget Start
2010-02-01
Budget End
2011-01-31
Support Year
30
Fiscal Year
2010
Total Cost
$201,313
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
Mitsche, Matthew A; Small, Donald M (2013) Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic ?-helices. J Lipid Res 54:1578-88
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
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

Showing the most recent 10 out of 235 publications