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Description

Proteins, which are remarkably complex machines, play a crucial role not only in the biological functions of your body but also in every living organism's processes. They serve as the fundamental units of life. As of now, there are approximately 100 million identified proteins, with discoveries being made regularly. Each protein possesses a distinctive three-dimensional shape that is essential to its functionality and purpose. However, determining a protein's precise structure is often a costly and lengthy endeavor, resulting in an understanding of only a small percentage of the proteins recognized by science. Addressing this growing disparity and developing methods to predict the structures of millions of yet-to-be-discovered proteins could significantly advance our ability to combat diseases, expedite the discovery of new treatments, and potentially unveil the secrets of life's mechanisms. The implications of such advancements could transform both medicine and our understanding of biology.

Description

Aurora utilizes principles of quantum mechanics and thermodynamics alongside a sophisticated continuous water model to assess the solvation effects on ligand binding affinities. This methodology is significantly different from the traditional scoring functions typically employed for predicting binding affinities. By integrating entropy and aqueous electrostatic contributions directly into the computations, Aurora's algorithms yield far more precise and reliable binding free energy values. The interaction between a ligand and a protein is fundamentally defined by the binding free energy value. This free energy (F) serves as a thermodynamic measure that correlates directly with the experimentally determined inhibition constant (IC50), influenced by factors such as electrostatic interactions, quantum effects, aqueous solvation forces, and the statistical characteristics of the molecules involved. Non-additivity in F arises primarily from two key components: the electrostatic and solvation energy, and the entropy, which together contribute to the complexity of ligand-protein interactions. Understanding these contributions is essential for the accurate prediction of binding affinities in drug design and molecular biology.

API Access

Has API No 

API Access

Has API No 

Screenshots View All

Screenshots View All

Integrations

Complete Yes 
Gemini Robotics Yes 
WeatherNext Yes 

Integrations

Complete No 
Gemini Robotics No 
WeatherNext No 

Pricing Details

No price information available.
Free Trial No 
Free Version No 

Pricing Details

No price information available.
Free Trial No 
Free Version No 

Deployment

Web-Based Yes 
On-Premises No 
iPhone App No 
iPad App No 
Android App No 
Windows No 
Mac No 
Linux No 
Chromebook No 

Deployment

Web-Based Yes 
On-Premises No 
iPhone App No 
iPad App No 
Android App No 
Windows No 
Mac No 
Linux No 
Chromebook No 

Customer Support

Business Hours No 
Live Rep (24/7) No 
Online Support Yes 

Customer Support

Business Hours Yes 
Live Rep (24/7) No 
Online Support Yes 

Types of Training

Training Docs No 
Webinars No 
Live Training (Online) No 
In Person No 

Types of Training

Training Docs No 
Webinars No 
Live Training (Online) No 
In Person No 

Vendor Details

Company Name

DeepMind

Founded

2010

Country

United Kingdom

Website

deepmind.com/research/case-studies/alphafold

Vendor Details

Company Name

Aurora Fine Chemicals

Founded

1990

Country

United States

Website

aurorafinechemicals.com/drug-discovery-software.html

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Product Features

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