Conformational distribution and α-helix to β-sheet transition of human amylin fragment dimer.

TL;DR: This review highlights recent studies that illustrate functional adjustment of protein conformational ensembles in the crowded cellular environment and focuses on the role of the ensemble in recognition of small- and macro-molecules and emerging concepts of protein dynamics in enzyme catalysis.

TL;DR: At atomistic and coarse-grained simulation studies of amyloid peptides in their monomeric, oligomersic, and fibrillar states are reviewed and particular emphasis is given to the challenges one faces to characterize at atomic level of detail the conformational space of disordered (poly)peptides and their aggregation.

TL;DR: This work reviews the most recent and important findings of amyloid cross-seeding behaviors from in vitro, in vivo, and in silico studies, and offers some personal perspectives on current major challenges and future research directions in this less-studied yet important field.

TL;DR: This chapter presents a brief introduction to REMD method and a practical application protocol with a case study of the dimerization of the 11-25 fragment of human islet amyloid polypeptide (hIAPP(11-25)), using the GROMACS software.

TL;DR: Islet amyloid is not the cause of type 2 diabetes, but it leads to β‐cell dysfunction and cell death, and contributes to the failure of islet cell transplantation.

TL;DR: This work uses isotope labeling and two-dimensional infrared spectroscopy to obtain a residue-specific structure for the complex of human amylin, the peptide responsible for islet amyloid formation in type 2 diabetes, with a known inhibitor, rat amyl in.

TL;DR: In vivo and in vitro measurements of membrane disruption indicate the rat version of IAPP(1-19), despite differing from hIAPP( 1-19) by the single substitution of Arg18 for His18, is significantly less toxic than hI APP(1 -19), in agreement with the low toxicity of the full-length rat IAPP peptide.

TL;DR: Investigating the conformations of Aβ(16-22) octamers in the absence and presence of a single-walled carbon nanotube (SWCNT) by performing extensive all-atom replica exchange molecular-dynamics simulations in explicit solvent provides evidence that SWCNT is likely to inhibit Aβ (16- 22) and full-length Aβ fibrillation.