2004 - Fellow of the American Academy of Arts and Sciences
1997 - Member of the National Academy of Sciences
1978 - Fellow of John Simon Guggenheim Memorial Foundation
His primary scientific interests are in Membrane protein, Crystallography, Transmembrane protein, Transmembrane domain and Biophysics. His Membrane protein study deals with Folding intersecting with Hydrophobic effect. His Crystallography research includes themes of Cholesterol, Bilayer, Halobacterium and Hydrocarbon.
Donald M. Engelman has included themes like Protein structure and Protein folding in his Transmembrane protein study. His Transmembrane domain research integrates issues from Alpha helix, Sequence, Ion channel, Phospholamban and Glycophorin. His Biophysics research is multidisciplinary, incorporating perspectives in Integral membrane protein and Membrane, Biochemistry, Lipid bilayer, Biological membrane.
Donald M. Engelman mostly deals with Biophysics, Transmembrane domain, Crystallography, Transmembrane protein and Membrane. His Biophysics study incorporates themes from Protein secondary structure, PH low-insertion peptide, Receptor, Lipid bilayer and Peptide. The Transmembrane domain study combines topics in areas such as Helix, Dimer, Stereochemistry, Hydrogen bond and Glycophorin.
His research in Crystallography intersects with topics in Neutron scattering, Bacteriorhodopsin, Folding, Molecule and Protein structure. He interconnects Integral membrane protein, Membrane protein, Amino acid and Cell biology in the investigation of issues within Transmembrane protein. In his study, Sodium is strongly linked to Chromatography, which falls under the umbrella field of Membrane.
His primary areas of investigation include Biophysics, Peptide, Membrane, Transmembrane domain and Lipid bilayer. His work on Membrane binding as part of general Membrane study is frequently connected to Conjugated system, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them. His Transmembrane domain study combines topics in areas such as Crystallography, Biological membrane and Transmembrane protein.
His Crystallography study integrates concerns from other disciplines, such as Membrane fluidity and Peripheral membrane protein. His research in Transmembrane protein intersects with topics in POPC, Membrane protein and Glycophorin. In his study, which falls under the umbrella issue of Lipid bilayer, Helix and Alpha helix is strongly linked to Bilayer.
Membrane protein, Biophysics, Transmembrane domain, Lipid bilayer and Peptide are his primary areas of study. His Membrane protein study is associated with Biochemistry. Donald M. Engelman has researched Biophysics in several fields, including Radiation oncology, Cell, Nanoparticle and In vivo.
As a part of the same scientific study, Donald M. Engelman usually deals with the Transmembrane domain, concentrating on Bilayer and frequently concerns with Protein structure. The various areas that Donald M. Engelman examines in his Lipid bilayer study include Stereochemistry, Circular dichroism and Peripheral membrane protein. His studies deal with areas such as Crystallography, Extracellular and Folding as well as Membrane.
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Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins.
D. M. Engelman;T. A. Steitz;A. Goldman.
Annual Review of Biophysics and Biophysical Chemistry (1986)
Membrane protein folding and oligomerization: the two-stage model.
J L Popot;D M Engelman.
A transmembrane helix dimer: structure and implications.
Kevin R. MacKenzie;James H. Prestegard;Donald M. Engelman.
Membranes are more mosaic than fluid
Donald M. Engelman.
The GxxxG motif: A framework for transmembrane helix-helix association
William P Russ;Donald M Engelman.
Journal of Molecular Biology (2000)
The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis
D.M. Engelman;T.A. Steitz.
Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
Barbara A. Lewis;Donald M. Engelman.
Journal of Molecular Biology (1983)
Helical Membrane Protein Folding, Stability, and Evolution
Jean-Luc Popot;Donald M. Engelman.
Annual Review of Biochemistry (2000)
Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions.
Alessandro Senes;Mark Gerstein;Donald M Engelman.
Journal of Molecular Biology (2000)
MicroRNA silencing for cancer therapy targeted to the tumour microenvironment
Christopher J. Cheng;Raman Bahal;Imran A. Babar;Imran A. Babar;Zachary Pincus;Zachary Pincus.
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