SASA (Solvent Accessible Surface Area) Analysis
Solvent accessible surface area (SASA) analysis is an important component of structural biology and biophysical chemistry. It provides an important basis for understanding the molecular interactions, stability and function of proteins, DNA and RNA. Understanding SASA is fundamental to predicting molecular behavior such as ligand binding, protein folding, and protein-protein interactions. With a commitment to excellence, innovation and scientific acumen, CD ComputaBio has become a pioneer in providing advanced analytical services to the scientific and pharmaceutical industries.
Our Algorithm
Protein SASA Calculation
Accurate determination of solvent accessible surface area for proteins.
Comprehensive analysis of protein dynamics and interactions.
Ligand SASA Calculation
Precise assessment of solvent-accessible surface area for ligands and small molecules.
Evaluation of ligand binding modes and binding site characteristics.
Complex SASA Calculation
Thorough analysis of solvent accessible surface area for protein-ligand complexes.
Insightful examination of binding interfaces and intermolecular interactions.
Our Services
Solvent accessible surface area (SASA) is a key parameter in molecular structure studies that describes the area around a macromolecule that is accessible to solvent molecules. It is an important indicator for understanding protein folding, ligand binding, and conformational changes and plays a key role in elucidating molecular interactions at the atomic level.
SASA Calculations
SASA analysis is a primary method for studying the behavior and function of biomolecules (such as proteins or nucleic acids) in solution by calculating their surface area in solution. The algorithm we use calculates the surface area of a molecule in solution by performing a fine-grained three-dimensional mesh of each atom of the molecule, including the solvent molecules surrounding it, and summing and integrating over them.
Structural Dynamics and Molecular Interaction Assessment
Structural Dynamics Assessment: Our team is adept at elucidating the soluble regions involved in protein-protein, protein-ligand, and protein-nucleic acid interactions, thus contributing to a comprehensive understanding of molecular recognition and binding mechanisms.
Assessment of molecular interactions: By combining SASA analysis with molecular dynamics simulations, we provide in-depth assessments of conformational changes and structural dynamics, which are critical for understanding macromolecular behavior under physiological conditions.
SASA-based Protein Interaction Analysis
SASA-based Protein Interaction Analysis Service: Using SASA data, we can reveal protein-protein and protein-ligand interactions, and reveal when, where, and how these interactions affect biological functions.
Hydrophobic and Hydrophilic Properties Analysis Service: Through SASA analysis, CD ComputaBio can help clients gain insight into the hydrophobic and hydrophilic properties of molecules, revealing their behavior in an aqueous environment and providing important data for drug design, protein engineering, and structure elucidation.
Delivery of Results
- Analysis Reports: used to present SASA's computational results, research findings, and possible explanatory scenarios.
- Raw computational and simulation data for further research and analysis by the client.
- Data graphs and live simulation animations tailored to the client's specific needs.
Workflow of Our Services
CD ComputaBio's SASA analysis service can help you deeply understand the behavior of molecules in solvents and their functions in molecular interactions, providing accurate data to support your research. Our professional team provides you with the best service with a scientific attitude and rigorous method, and your satisfaction is our highest pursuit. Contact us now for more details on our services!
References:
- Devaurs D, et al. Computational modeling of molecular structures guided by hydrogen-exchange data. Journal of the American Society for Mass Spectrometry, 2022, 33(2): 215-237.
- Hayakawa D, et al. A molecular interaction field describing nonconventional intermolecular interactions and its application to protein–ligand interaction prediction. Journal of Molecular Graphics and Modelling, 2020, 96: 107515.
- Dash R, et al. Structural and dynamic characterizations highlight the deleterious role of SULT1A1 R213H polymorphism in substrate binding. International journal of molecular sciences, 2019, 20(24): 6256.
* For Research Use Only.
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