22 research outputs found
Complexity of Some Interesting (Chemical) Graphs
Get PDFComplexity of some interesting polycyclic graphs is expressed in
terms of the corresponding spanning trees. Graphs considered were
a selection of all connected graphs with four and five vertices, graphs composed of two parts, or more parts, connected by a single edge, the Petersen graph, the Blanuša graph, the Desargues-Levy graph and the Schlegel graph of buckminsterfullerene
Complexity of Some Interesting (Chemical) Graphs
Get PDFComplexity of some interesting polycyclic graphs is expressed in
terms of the corresponding spanning trees. Graphs considered were
a selection of all connected graphs with four and five vertices, graphs composed of two parts, or more parts, connected by a single edge, the Petersen graph, the Blanuša graph, the Desargues-Levy graph and the Schlegel graph of buckminsterfullerene
Comment on “Can a Continuum Solvent Model Reproduce the Free Energy Landscape of a β-Hairpin Folding in Water?” The Poisson−Boltzmann Equation
No full textElastic Bag Model for Molecular Dynamics Simulations of Solvated Systems: Application to Liquid Argon
No full textSimulation Study of Stapled Alpha-Helical P53 Peptide Analogs:probing the Relationship between Structural Stability and Biological Potency
No full textPredicting GPCR Promiscuity Using Binding Site Features
No full textG protein-coupled
receptors (GPCRs) represent a large family of
signaling proteins that includes many therapeutic targets. GPCR ligands
include odorants, tastants, and neurotransmitters and vary in size
and properties. Dramatic chemical diversity may occur even among ligands
of the same receptor. Our goal is to unravel the structural and chemical
features that determine GPCRs’ promiscuity toward their ligands.
We perform statistical analysis using more than 30 descriptors related
to the sequence, physicochemical, structural, and energetic properties
of the GPCR binding siteswe find that the chemical variability
of antagonists significantly correlates with the binding site hydrophobicity
and anticorrelates with the number of hydrogen bond donors in the
binding site. The number of disulfide bridges in the extracellular
region of a receptor anticorrelates with the range of molecular weights
of its antagonists, highlighting the role of the entrance pathway
in determining the size selectivity for GPCR antagonists. The predictive
capability of the model is successfully validated using a separate
set of GPCRs, using either X-ray structures or homology models
PB2349: A PHASE 1, OPEN-LABEL, MULTICENTER, DOSE-ESCALATION STUDY OF SGR-1505 AS MONOTHERAPY IN SUBJECTS WITH MATURE B-CELL MALIGNANCIES
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