Vibrational analysis of capped [Leu]enkephalin
Literature Information
Tim M. Watson, Jonathan D. Hirst
The enkephalins are peptides with important biological activity. They are much more conformationally flexible than morphine, yet they bind to similar receptors with greater binding affinity. Their structures are therefore of particular interest. In this work we study the gas-phase low energy conformers of capped [Leu]enkephalin using the EDF1 density functional with the 6-31+G* basis set. The lowest energy structure found is a single β-bend structure. Calculated vibrational spectra indicate considerable scope for determination of low energy conformers from experiment.
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Physical Chemistry Chemical Physics

Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions. The journal has a broad scope and welcomes contributions spanning experiment, theory, computation and data science. Topical coverage includes spectroscopy, dynamics, kinetics, statistical mechanics, thermodynamics, electrochemistry, catalysis, surface science, quantum mechanics, quantum computing and machine learning. Interdisciplinary research areas such as polymers and soft matter, materials, nanoscience, energy, surfaces/interfaces, and biophysical chemistry are welcomed if they demonstrate significant innovation and/or insight into physical chemistry. Joined experimental/theoretical studies are particularly appreciated when complementary and based on up-to-date approaches.











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