The Conformation and Assignment of the Proton NMR Spectrum in Water of DX600, a Bioactive Peptide with a Random Coil Conformation | Zendy

Wayne E. Steinmetz | Zendy; Timothy N. Carrell | Zendy; Richard B. Peprah | Zendy

Open Access

The Conformation and Assignment of the Proton NMR Spectrum in Water of DX600, a Bioactive Peptide with a Random Coil Conformation

Author(s) -

Wayne E. Steinmetz,

Timothy N. Carrell,

Richard B. Peprah

Publication year - 2011

Publication title -

international journal of spectroscopy

Language(s) - English

Resource type - Journals

eISSN - 1687-9457

pISSN - 1687-9449

DOI - 10.1155/2011/296256

Subject(s) - random coil , chemistry , peptide , conformational isomerism , molecular dynamics , proton , crystallography , peptide conformation , hydrogen bond , knot (papermaking) , proton nmr , nuclear magnetic resonance spectroscopy , yield (engineering) , stereochemistry , computational chemistry , circular dichroism , materials science , molecule , organic chemistry , physics , biochemistry , thermodynamics , quantum mechanics , composite material

DX600, a small peptide with 26 residues, is a potent, highly selective inhibitor of angiotensin converting enzyme 2 (ACE2). A range of NMR methods including TOCSY and ROESY yield an assignment of its proton spectrum in water and constraints on its conformation. Constrained molecular dynamics simulations of solvated DX600 show that the peptide's most abundant conformer adopts a predominantly random coil conformation. Constrained by the disulfide bond, its backbone defines an overhand knot with frayed ends

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