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

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.

Documentation