BIOISIS
BIOISIS analyzes small angle X-ray scattering (SAXS) data to characterize the structural dynamics and interactions of biological macromolecules, including proteins and protein-ssDNA complexes such as Replication Protein A (RPA).
Key Features:
- Data Integration: BIOISIS integrates SAXS experimental data with computational simulations to provide a holistic view of macromolecular structures.
- Structural Dynamics Analysis: BIOISIS examines flexibility and orientation changes in protein domains relevant to functional mechanisms.
Scientific Applications:
- RPA structural dynamics: Analysis of Replication Protein A (RPA), including the RPA70 heterotrimeric protein and constructs RPA70AB and RPA70NAB, to investigate domain organization and flexibility.
- Interdomain flexibility: Identification of significant flexibility between the A and B domains of RPA70AB relevant to its function.
- ssDNA binding effects and domain independence: Observation that ssDNA binding reduces flexibility between RPA70AB domains while RPA70N remains structurally independent, supporting its role as a protein recruitment module.
Methodology:
Integration of SAXS experimental data with computational simulations.
Topics
Collections
Details
- Cost:
- Free of charge
- Tool Type:
- web application
- Operating Systems:
- Linux, Windows, Mac
- Added:
- 3/5/2015
- Last Updated:
- 12/10/2018
Operations
Data Inputs & Outputs
Analysis
Inputs
Outputs
Publications
Pretto DI, Tsutakawa S, Brosey CA, Castillo A, Chagot M, Smith JA, Tainer JA, Chazin WJ. Structural Dynamics and Single-Stranded DNA Binding Activity of the Three N-Terminal Domains of the Large Subunit of Replication Protein A from Small Angle X-ray Scattering. Biochemistry. 2010;49(13):2880-2889. doi:10.1021/bi9019934. PMID:20184389. PMCID:PMC2847624.
DOI: 10.1021/bi9019934