Protein Structure Characterization Service

Protein structure characterization is a critical process in structural biology, aiming to elucidate the three-dimensional arrangement of atoms within a protein molecule. By utilizing advanced techniques such as X-ray crystallography, nuclear magnetic resonance (NMR), cryo-electron microscopy (Cryo-EM), and cross-linking mass spectrometry (XL-MS), protein structure characterization provides high-resolution structural data that facilitate the study of protein folding mechanisms, ligand binding, and protein-protein interactions. Protein structure characterization typically begins with protein expression and purification, followed by selecting an appropriate analytical method based on the protein's properties. For instance, X-ray crystallography or Cryo-EM is ideal for resolving large protein complexes, while NMR and XL-MS are better suited for studying dynamic or flexible regions. The resulting structural data are used to determine spatial configurations, interaction sites, and conformational dynamics of proteins. Protein structure characterization plays an essential role in drug design, biomarker identification, and studying the molecular mechanisms underlying various biological processes. For example, it can reveal the mechanisms of receptor-ligand interactions or provide a deeper understanding of complex protein conformations (such as knotted proteins) and their effects on stability and function. Protein structure characterization is the foundation for understanding protein function and is an indispensable step in drug design, biomarker discovery, and exploring molecular mechanisms.

 



Lan, T. et al. Food Chem X. 2024. 

Figure 1. Techniques for Protein Structure Characterization

 

Services at MtoZ Biolabs

MtoZ Biolabs is an international contract research organization (CRO) specializing in advanced services in proteomics, metabolomics, and biopharmaceutical analysis. Our protein structure characterization service employs cutting-edge technologies such as mass spectrometry (MS), nuclear magnetic resonance (NMR), and X-ray crystallography to deliver high-resolution three-dimensional protein structural data. Our analytical team, composed of highly experienced scientists, is dedicated to providing customized solutions tailored to diverse research needs. We are committed to advancing scientific research and enabling clients to achieve breakthrough results in drug design, biomarker discovery, and functional studies.

 

Service Advantages

1. High-Precision Structural Analysis Capabilities 

MtoZ Biolabs’protein structure characterization service utilizes industry-leading techniques such as X-ray crystallography, nuclear magnetic resonance (NMR), and cryo-electron microscopy (Cryo-EM), providing clients with high-resolution, three-dimensional protein structural data. These techniques ensure precise analysis of complex protein structures, especially in areas such as protein folding, ligand binding, and protein-protein interactions, all vital components of a comprehensive protein structure characterization service.

 

2. Customized Solutions for Diverse Protein Types  

MtoZ Biolabs’protein structure characterization service is designed to offer flexible, tailored solutions for a broad spectrum of protein types, including membrane proteins, large complexes, and intrinsically disordered proteins. The service is adaptable to the specific challenges posed by each protein class, ensuring that even the most difficult-to-characterize proteins receive the attention and precision they need for accurate structural analysis.

 

3. Accelerated Discovery with Cutting-Edge Technology  

Through its advanced protein structure characterization service, MtoZ Biolabs helps accelerate the discovery process for drug design, biomarker identification, and functional studies. By leveraging the latest in structural biology technologies, the service enhances understanding of molecular mechanisms, driving faster and more informed decisions in both research and development.

 

Case Study

Case 1: This study provides structural insights into the apelin receptor-G protein stoichiometry, revealing how the receptor interacts with G proteins and the mechanisms behind their coupling. Using advanced techniques such as cryo-EM, the research uncovers the precise arrangement of G protein subunits within the receptor complex, offering critical insights into receptor-G protein interactions. These findings enhance our understanding of G protein-coupled receptor signaling, which is essential for developing targeted therapeutics. Protein structure characterization service offers detailed structural analysis of protein complexes using state-of-the-art techniques like cryo-EM and X-ray crystallography, helping to uncover the molecular details of receptor signaling and drug design.

 



Yue, Y. et al. Nat Struct Mol Biol. 2022.

Figure 2. Cryo-EM-Based Structural Insight into Apelin Receptor-G Protein Stoichiometry

 

Case 2: This study explores the conformational and structural characterization of knotted proteins, which are known for their complex topologies that include knot-like structures within their polypeptide chains. Using advanced techniques like X-ray crystallography and NMR spectroscopy, the research provides detailed insights into how these knots influence protein stability, folding, and function. Understanding the structural dynamics of knotted proteins is crucial for comprehending their biological roles and potential therapeutic applications. Protein structure characterization service offers specialized analysis of complex protein structures, including knotted proteins, using cutting-edge methods such as X-ray crystallography, NMR, and cryo-EM. This service provides high-resolution structural data essential for understanding the folding mechanisms and functional implications of such unique proteins.

 



Jeanne, Dit, Fouque, K. et al. Biochemistry. 2024.

Figure 3. Conformational Analysis of Knotted Proteins Using X-ray Crystallography

 

FAQ

Q1: In the process of protein structure identification, how can cross-linking mass spectrometry (XL-MS) be used to effectively identify the spatial configuration of proteins and the interaction sites within protein complexes?

Answer: XL-MS is a powerful technique for protein structure characterization, as it allows for the identification of spatial proximities between residues in a protein or protein complex. By covalently linking interacting proteins or protein domains and analyzing the cross-linked peptides through mass spectrometry, we can deduce both the 3D structure and interaction networks within the complex. This method is especially valuable in capturing transient or weak interactions that may be difficult to observe with traditional methods like X-ray crystallography or cryo-EM. For accurate protein structure identification, integrating XL-MS with other structural biology techniques can provide a comprehensive view of protein conformations, aiding in the understanding of functional mechanisms. Our protein structure characterization service leverages XL-MS to deliver detailed insights into protein interactions, providing critical information for drug discovery and therapeutic development.

 

Deliverables

1. Comprehensive Experimental Details

2. Materials, Instruments, and Methods

3. Relevant Liquid Chromatography and Mass Spectrometry Parameters

4. The Detailed Information of Protein Structure Characterization

5. Mass Spectrometry Image

6. Raw Data