Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Exploratory/Developmental Grants (R21)
Project #
1R21AI047153-01
Application #
6086400
Study Section
Molecular and Cellular Biophysics Study Section (BBCA)
Program Officer
Plaeger, Susan F
Project Start
2000-09-30
Project End
2001-09-29
Budget Start
2000-09-30
Budget End
2001-09-29
Support Year
1
Fiscal Year
2000
Total Cost
$225,880
Indirect Cost
Name
Michigan State University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
193247145
City
East Lansing
State
MI
Country
United States
Zip Code
48824
Liang, S; Ratnayake, P U; Keinath, C et al. (2018) Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains. Biochemistry 57:1219-1235
Weliky, David P (2015) A new understanding of antibiotic action via solid-state NMR of cells with uniform isotopic labeling. Biophys J 108:1314
Xie, Li; Jia, Lihui; Liang, Shuang et al. (2015) Multiple locations of peptides in the hydrocarbon core of gel-phase membranes revealed by peptide (13)C to lipid (2)H rotational-echo double-resonance solid-state nuclear magnetic resonance. Biochemistry 54:677-84
Ghosh, Ujjayini; Xie, Li; Jia, Lihui et al. (2015) Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis. J Am Chem Soc 137:7548-51
Gabrys, Charles M; Qiang, Wei; Sun, Yan et al. (2013) Solid-state nuclear magnetic resonance measurements of HIV fusion peptide 13CO to lipid 31P proximities support similar partially inserted membrane locations of the * helical and * sheet peptide structures. J Phys Chem A 117:9848-59
Xie, Li; Ghosh, Ujjayini; Schmick, Scott D et al. (2013) Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR. J Biomol NMR 55:11-7
Vogel, Erica P; Weliky, David P (2013) Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy. Biochemistry 52:4285-7
Ghosh, Ujjayini; Xie, Li; Weliky, David P (2013) Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR. J Biomol NMR 55:139-46
Tristram-Nagle, Stephanie; Chan, Rob; Kooijman, Edgar et al. (2010) HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics. J Mol Biol 402:139-53
Schmick, Scott D; Weliky, David P (2010) Major antiparallel and minor parallel ? sheet populations detected in the membrane-associated human immunodeficiency virus fusion peptide. Biochemistry 49:10623-35

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