☰ Chemistry Tree

David P. Weliky

Affiliations:

1997-

Michigan State University, East Lansing, MI

Area:

Biochemistry, NMR

Website:

https://www.chemistry.msu.edu/faculty-research/faculty-members/david-p-weliky/

Google:

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Parents

Takeshi Oka	grad student	1990-1995	Chicago
Robert Tycko	post-doc	1995-1997	NIH (Physics Tree)

Children

Michele L. Bodner	grad student	2006	Michigan State
Paul Parkanzky	grad student	2006	Michigan State
Matthew A. Gave	grad student	2007	Michigan State
Zhaoxiong Zheng	grad student	2007	Michigan State
Jaime L. Curtis-Fisk	grad student	2009	Michigan State
Wei Qiang	grad student	2009	Michigan State
Scott Schmick	grad student	2012	Michigan State
Erica P. Vogel	grad student	2012	Michigan State
Matthew J. Nethercott	grad student	2006-2012	Michigan State
Koyeli Banerjee	grad student	2014	Michigan State

Collaborators

BETA: Related publications

Publications

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Zhang Y, Ghosh U, Xie L, et al. (2023) Lipid acyl chain protrusion induced by the influenza virus hemagglutinin fusion peptide detected by NMR paramagnetic relaxation enhancement. Biophysical Chemistry. 299: 107028
Rokonujjaman M, Sahyouni A, Wolfe R, et al. (2022) A large HIV gp41 construct with trimer-of-hairpins structure exhibits V2E mutation-dominant attenuation of vesicle fusion and helicity very similar to V2E attenuation of HIV fusion and infection and supports: (1) hairpin stabilization of membrane apposition with larger distance for V2E; and (2) V2E dominance by an antiparallel β sheet with interleaved fusion peptide strands from two gp41 trimers. Biophysical Chemistry. 293: 106933
Ghosh U, Weliky DP. (2021) Rapid H NMR Transverse Relaxation of Perdeuterated Lipid Acyl Chains of Membrane with Bound Viral Fusion Peptide Supports Large-Amplitude Motions of These Chains That Can Catalyze Membrane Fusion. Biochemistry
Jain V, Shelby T, Patel T, et al. (2021) A Bimodal Nanosensor for Probing Influenza Fusion Protein Activity Using Magnetic Relaxation. Acs Sensors
Ghosh U, Weliky DP. (2020) H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pH. Biochimica Et Biophysica Acta. Biomembranes. 183404
Ranaweera A, Ratnayake PU, Ekanayaka EAP, et al. (2019) Hydrogen-deuterium exchange supports independent membrane-interfacial fusion peptide and transmembrane domains in subunit 2 of influenza virus hemagglutinin protein, a structured and aqueous-protected connection between the fusion peptide and soluble ectodomain, and the importance of membrane apposition by the trimer-of-hairpins structure. Biochemistry
Ranaweera A, Ratnayake PU, Weliky DP. (2018) The Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively Correlated with Membrane Fusion. Biochemistry
Liang S, Ratnayake P, Keinath C, et al. (2018) Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain. Biochemistry
Weliky D. (2018) NMR Contacts between the HIV Fusion Peptide and Lipid Support a Beta-Bowl Membrane Topology of the Peptide with Thermodynamic Preference for Peptide/Cholesterol Contact Biophysical Journal. 114: 552a
Ratnayake PU, Prabodha Ekanayaka EA, Komanduru SS, et al. (2016) Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide make significant contributions to fusion of membrane vesicles. Protein Expression and Purification. 117: 6-16

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