PH Sensitivity of the SERF1a Conformational Ensemble.

ABSTRACT: The MOAG-4/SERF class of proteins is a positive regulator of the aggregate formation of amyloid proteins that play an important role in the origin of numerous age-related diseases. In this class of proteins, previous structural studies showed that SERF1a is a very flexible protein, containing at least one α-helical region. The present work proposes the first description of the conformational space of SERF1a at two pH values (6 and 6.8) using nuclear magnetic resonance (NMR) and small-angle X-ray scattering (SAXS). SERF1a NMR conformations have been generated using the CYANA-FLYA procedure as well as the TAiBP (Threading-Augmented interval Branch-and-Prune) procedure, based on the systematic enumeration of protein conformations within an original distance geometry scheme. The generated conf

SUBMITTER: Huang SY 

PROVIDER: S-EPMC12824765 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature