Computational investigation of retro‐isomer equilibrium structures: Intrinsically disordered, foldable, and cyclic peptides. Issue 1 (9th August 2019)

• Record Type: Journal Article
• Authors: Zerze, Gül H.; Stillinger, Frank H.; Debenedetti, Pablo G.
• Is Part Of: FEBS letters. Volume 594:Issue 1(2020)
• Page Start: 104
• Page End: 113
• Publication Date: 2019-08-09
• Subjects: Aβ -- cyclic peptides -- intrinsically disordered peptides -- p53 -- peptidomimetics -- retro peptides; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.13558
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : We use all‐atom modeling and advanced‐sampling molecular dynamics simulations to investigate quantitatively the effect of peptide bond directionality on the equilibrium structures of four linear (two foldable, two disordered) and two cyclic peptides. We find that the retro forms of cyclic and foldable linear peptides adopt distinctively different conformations compared to their parents. While the retro form of a linear intrinsically disordered peptide with transient secondary structure fails to reproduce a secondary structure content similar to that of its parent, the retro form of a shorter disordered linear peptide shows only minor differences compared to its parent. Abstract :