Related Experiment Video
Updated: Jan 28, 2026
04:37
High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
3.1K
pH Sensitivity of the SERF1a Conformational Ensemble
Shu-Yu Huang1, Orion Shih2, U-Ser Jeng2,3
1Research Center for Applied Sciences, Academia Sinica, Taipei 11529, Taiwan.
ACS Omega
|January 26, 2026
Summary
The SERF1a protein
Area of Science:
- Structural biology
- Biophysics
- Molecular biology
Background:
- The MOAG-4/SERF protein class positively regulates amyloid aggregate formation, implicated in age-related diseases.
- SERF1a is a flexible protein with at least one alpha-helical region, playing a role in amyloid aggregation.
Purpose of the Study:
- To characterize the conformational space of SERF1a at pH 6 and 6.8.
- To investigate the conformational dynamics and potential binding sites of SERF1a.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy to determine protein structure and dynamics.
- Small-Angle X-ray Scattering (SAXS) to assess overall protein conformation in solution.
- Computational methods including CYANA-FLYA and Threading-Augmented interval Branch-and-Prune (TAiBP) for conformation generation.
- Pepsi-SAXS for fitting experimental SAXS data with generated conformations.
Main Results:
- At pH 6.8, NMR and SAXS data showed good agreement, indicating a defined conformation.
- At pH 6, evidence suggests conformational exchange between compact and extended states, with altered helical stability.
- The N-terminal region of SERF1a exhibits potential binding pockets, particularly interacting with alpha-synuclein.
- The TAiBP procedure provided a more comprehensive exploration of SERF1a's conformational space and dynamics.
Conclusions:
- SERF1a exhibits pH-dependent conformational flexibility, potentially influencing its role in age-related diseases.
- The observed conformational changes at acidic pH may relate to SERF1a's function in nucleoli.
- SERF1a's N-terminal region is a key site for interactions, including with alpha-synuclein.
- Advanced computational methods like TAiBP enhance the understanding of protein dynamics and conformational ensembles.
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