At CD ComputaBio, we specialize in providing comprehensive Protein Infrared (IR) Spectrum Characterisation services. Leveraging advanced computational modeling techniques, our service aims to assist researchers in understanding protein structures and dynamics through their infrared spectra. Our commitment to precision and innovation ensures that we deliver reliable, high-quality results tailored to meet your research needs.
Backgroud
Infrared spectroscopy is a powerful analytical technique used to probe the molecular composition and structure of proteins. By analyzing the IR spectrum, researchers can obtain detailed information about protein secondary structures, such as alpha-helices and beta-sheets, and their dynamic behaviors. This method has wide applications in fields such as biochemistry, pharmaceuticals, and materials science. Recognizing the importance of accurate protein characterization in these studies, CD ComputaBio has developed a specialized service to address this need.
Figure 1. Protein IR Spectrum Characterisation Service.( Lozano M, et al.2017)
Our Service
CD ComputaBio offers a comprehensive suite of services related to Protein IR Spectrum Characterisation:
Service s
D escription
IR Spectrum Acquisition
IR Spectrum Acquisition: Using advanced IR spectroscopy instruments, we acquire high-resolution spectra of your protein samples.
Computational Modeling
We employ sophisticated computational models to simulate the IR spectra of proteins, accounting for their specific structural features.
Data Analysis and Interpretation
Our team of experts analyzes the spectral data to provide insights into the secondary and tertiary structures of proteins and their dynamic changes.
Custom Solutions
We offer tailored services to meet specific research needs, including the study of protein-ligand interactions, protein folding/unfolding mechanisms, and more.
Applications
The Protein IR Spectrum Characterisation Service provided by CD ComputaBio has a broad range of applications, including but not limited to:
Structural Biology: Understanding the specific folding patterns and conformations of proteins.
Biopharmaceutical Development: Characterizing therapeutic proteins and antibodies to ensure their structural integrity and efficacy.
Enzyme Catalysis Research: Investigating the dynamic structural changes of enzymes during catalysis.
Protein-Protein Interactions: Studying how proteins interact with each other and with other biomolecules.
Our Algorithm
Molecular Dynamics (MD)
These simulations track the physical movements of atoms and molecules over time, providing dynamic structural information of proteins.
Normal Mode Analysis (NMA)
This technique helps in understanding the collective movements of atoms within a protein, enhancing the interpretation of IR spectra.
Machine Learning
We integrate machine learning algorithms to predict and refine protein IR spectra, leveraging large datasets to improve predictive accuracy.
Sample Requirements
To ensure the highest quality of Protein IR Spectrum Characterisation, we recommend the following sample preparation guidelines:
Protein Concentration: Ideally, samples should have a protein concentration of at least 1 mg/mL.
Purity: Samples must be free from contaminants like salts, detergents, and other interfering substances.
Volume: A minimum volume of 100 µL is required for reliable IR spectrum acquisition.
Form: Samples can be provided in either liquid form or lyophilized powder.
Results Delivery
Upon completion of the Protein IR Spectrum Characterisation, CD ComputaBio provides a comprehensive results package that includes:
High-Resolution IR Spectra: Raw and processed spectral data.
Structural Analysis Reports: Detailed interpretations of the IR spectra, highlighting key structural features and dynamics.
Comparative Analysis: If requested, comparative analysis with known protein structures or previous samples.
Our Advantages
Advanced Technology
We utilize cutting-edge instruments and algorithms to deliver precise and accurate results.
Customized Solutions
We work closely with our clients to tailor services that meet their specific research goals and requirements.
Comprehensive Support
From sample preparation to data interpretation, we offer full support throughout the entire process.
The Protein IR Spectrum Characterisation Service by CD ComputaBio is designed to provide researchers with a deep understanding of protein structures and their dynamic behaviors. By combining advanced IR spectroscopy with state-of-the-art computational modeling, we offer unparalleled insights that can significantly enhance your research outcomes. Whether you are studying protein folding mechanisms, drug-protein interactions, or structural biology, our service is equipped to meet your highest expectations.
Frequently Asked Questions
How does computational modeling assist in this characterisation service?
Computational modeling is essential in Protein IR Spectrum Characterisation Service. It helps predict the theoretical IR spectra based on the proposed protein structure and chemical composition. By using quantum mechanical calculations and molecular dynamics simulations, models can simulate the vibrations of the chemical bonds and predict the corresponding IR absorption frequencies and intensities. This allows for a comparison between the experimentally obtained spectra and the computationally predicted ones, aiding in the interpretation of the data. For instance, if there are differences between the experimental and predicted spectra, it can indicate
What types of proteins are suitable for IR spectrum characterisation?
Most proteins, regardless of their size, function, or source, can be potentially characterised using IR spectroscopy. This includes enzymes, structural proteins, membrane proteins, and proteins involved in various biological processes. However, the sample preparation methods might vary depending on the protein's properties. Soluble proteins are often easier to handle, but membrane proteins might require special detergents or lipid environments to maintain their native structure. Let's say you have a newly discovered protein from a bacterial strain. IR spectroscopy can be used to understand its structural characteristics and compare them to similar proteins.
What Types of Proteins Can Be Characterized Using This Service?
The Protein IR Spectrum Characterization Service can accommodate a wide variety of proteins, including:
Native proteins: Naturally occurring proteins isolated from biological sources.
Membrane proteins: Proteins embedded in cellular membranes, crucial for cell signaling and transport.
Enzymes: Protein catalysts whose activity can be monitored through conformational changes upon substrate binding.
Aggregates: To study the behavior and alterations in protein aggregates, which are significant in diseases like Alzheimer's.
How long does the characterisation process typically take?
The time required for the characterisation can vary depending on factors such as sample preparation, data collection time, and data analysis complexity.
On average, it can take anywhere from a few days to a couple of weeks. Simple samples with straightforward analysis might yield results faster, while more complex proteins or those requiring extensive data processing could take longer.
Reference
Lozano M, Rodríguez-Ulibarri P, Echeverría J C, et al. Mid-infrared spectroscopy (MIR) for simultaneous determination of fat and protein content in meat of several animal species. Food Analytical Methods, 2017, 10(10): 3462-3470.
For research use only. Not intended for any clinical use.
Figure 1. Protein IR Spectrum Characterisation Service.( Lozano M, et al.2017) 
