Christopher M. MacDermaid
Temple University
20 Papers
27 Citations
Christopher M. MacDermaid is an academic researcher from Temple University. The author has contributed to research in topics: Chemistry & Stratum corneum. The author has an hindex of 11, co-authored 19 publications. Previous affiliations of Christopher M. MacDermaid include Central Michigan University & GlaxoSmithKline.
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Papers
Computational design of a protein crystal
Christopher J. Lanci,Christopher M. MacDermaid,Seung-gu Kang,Rudresh Acharya,Benjamin North,Xi Yang,X. Jade Qiu,William F. DeGrado,Jeffery G. Saven +8 more
TL;DR: A computational approach is presented for the design of proteins that self-assemble in three dimensions to yield macroscopic crystals and has potential applications to the de novo design of nanostructured materials and to the modification of natural proteins to facilitate X-ray crystallographic analysis.
Chiral synthesis of LSD1 inhibitor GSK2879552 enabled by directed evolution of an imine reductase
Markus Schober,Christopher M. MacDermaid,Anne A. Ollis,Sandy S. Chang,Diluar Khan,Joseph Hosford,Jonathan Latham,Leigh Anne F. Ihnken,Murray J. B. Brown,Douglas E. Fuerst,Mahesh J. Sanganee,Gheorghe-Doru Roiban +11 more
- 16 Sep 2019
TL;DR: A wild-type imine reductase that was engineered to perform reductive amination with concomitant substrate amine resolution to give a commercially relevant manufacturing process to lysine-specific demethylase-1 inhibitor GSK2879552 is described.
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Molecular dynamics simulations of cholesterol-rich membranes using a coarse-grained force field for cyclic alkanes.
Christopher M. MacDermaid,Hemant K. Kashyap,Russell DeVane,Wataru Shinoda,Jeffery B. Klauda,Michael L. Klein,Giacomo Fiorin +6 more
TL;DR: A new CG force field for cholesterol is presented which performs with precision comparable to atomistic force fields in predicting the properties of cholesterol-rich phospholipid bilayers, including area per lipid, bilayer thickness, tail order parameter, increase in bending rigidity, and propensity to form liquid-ordered domains in ternary mixtures.
Engineering complementary hydrophobic interactions to control β-hairpin peptide self-assembly, network branching, and hydrogel properties.
Sameer Sathaye,Huixi Zhang,Cem Sonmez,Joel P. Schneider,Christopher M. MacDermaid,Christopher D Von Bargen,Jeffery G. Saven,Darrin J. Pochan +7 more
TL;DR: Molecular dynamics simulations provide a molecular picture of interpeptide interactions within the assembly that is consistent with the branching propensity of MAX1 vs LNK1 and in agreement with experimental observations.
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Electrostatic polarization is crucial for reproducing pKa shifts of carboxylic residues in Turkey ovomucoid third domain.
TL;DR: The studies have demonstrated that the Poisson-Boltzmann solvation model is more than adequate in reproducing pKa shifts, and confirmed previously reported conclusions that p Ka shifts for protein residues are controlled by the immediate environment of the residues in question, as opposed to long-range interactions in proteins.
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