M
Michael F. Mesleh
Researcher at Broad Institute
Publications - 37
Citations - 2795
Michael F. Mesleh is an academic researcher from Broad Institute. The author has contributed to research in topics: Residual dipolar coupling & Nuclear magnetic resonance spectroscopy. The author has an hindex of 21, co-authored 36 publications receiving 2546 citations. Previous affiliations of Michael F. Mesleh include Cubist Pharmaceuticals & University of Maryland Biotechnology Institute.
Papers
More filters
Journal ArticleDOI
Characterization of the Prion Protein Binding Properties of Antisense Oligonucleotides
Andrew G. Reidenbach,Eric Vallabh Minikel,Hien T Zhao,Stacy G Guzman,Stacy G Guzman,Stacy G Guzman,Alison Leed,Michael F. Mesleh,Holly B. Kordasiewicz,Stuart L. Schreiber,Stuart L. Schreiber,Sonia M Vallabh +11 more
TL;DR: The findings support the further development of PrP-lowering ASOs and of CSF PrP as a pharmacodynamic biomarker and salt dependence of the affinity measured by isothermal titration calorimetry are supported.
Journal ArticleDOI
Dipolar Waves as NMR maps of helices in proteins.
TL;DR: Dipolar Waves describe the periodic variation in the magnitudes of dipolar couplings in the backbone of a protein as a function of residue number and provide a tool for accurately describing helices and a step towards high throughput structure determination of proteins.
Book ChapterDOI
NMR experiments on aligned samples of membrane proteins.
A.A. De Angelis,David H. Jones,Christopher V. Grant,Sang Ho Park,Michael F. Mesleh,Stanley J. Opella +5 more
TL;DR: NMR methods can be used to determine the structures of membrane proteins and Lipids can be chosen so that protein-containing micelles, bicells, or bilayers are available as samples.
Journal ArticleDOI
Structure, Topology, and Dynamics of Myristoylated Recoverin Bound to Phospholipid Bilayers†
TL;DR: These results demonstrate that membrane binding by recoverin is achieved primarily by insertion of the myristoyl group inside the bilayer with apparently little rearrangement of the protein structure.
Journal ArticleDOI
Structure and dynamics of a membrane protein in micelles from three solution NMR experiments.
TL;DR: Three solution NMR experiments on a uniformly 15N labeled membrane protein in micelles provide sufficient information to describe the structure, topology, and dynamics of its helices, as well as additional information that characterizes the principal features of residues in terminal and inter-helical loop regions.