Home / Services / Protein Engineering and Optimization / Protein Structure Determination / Protein Structure Characterization Services

Protein Structure Characterization Services

Online Inquiry

Protein structure characterization services provide detailed insights into the three-dimensional architecture of proteins, which is essential for understanding their function, interactions, and mechanisms of action. Our comprehensive services cover a range of techniques from initial consultation to final analysis, ensuring accurate and high-resolution structural data tailored to your research needs.

Three-dimensional structures of proteins that show native metal-binding properties. (VM Bolanos-Garcia, et al.,2006)

Overview Service Process Examples and Solutions Frequently Asked Questions


Protein structure characterization involves determining the three-dimensional arrangement of atoms within a protein. This information is crucial for elucidating protein function, designing drugs, and understanding disease mechanisms. Our services utilize state-of-the-art technologies and methodologies, including X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, cryo-electron microscopy (cryo-EM), and computational modeling, to provide detailed structural insights.

Methods for Protein Structure Characterization

Method Description Applicable Scenarios
X-ray Crystallography Determines the atomic structure of a protein by analyzing the diffraction patterns of X-rays passing through a crystallized protein sample. Suitable for high-resolution structure determination of well-crystallized proteins, commonly used in drug discovery and structural biology.
Nuclear Magnetic Resonance (NMR) Spectroscopy Uses magnetic fields and radio waves to determine the structure of proteins in solution, providing information on protein dynamics and interactions. Ideal for studying proteins that are difficult to crystallize, analyzing protein dynamics, and investigating protein-ligand interactions.
Cryo-Electron Microscopy (Cryo-EM) Captures images of proteins at near-atomic resolution by rapidly freezing the sample and examining it with an electron microscope. Suitable for studying large protein complexes, membrane proteins, and samples that are challenging to crystallize, widely used in structural biology.
Small Angle X-ray Scattering (SAXS) Measures the scattering of X-rays as they pass through a protein solution, providing information about the overall shape and size of the protein. Useful for studying the structure of proteins in solution, analyzing conformational changes, and investigating protein complexes.
Circular Dichroism (CD) Spectroscopy Measures the differential absorption of circularly polarized light to provide information about the secondary structure content of proteins. Ideal for studying protein folding, conformational changes, and thermal stability, often used in protein engineering and quality control.
Mass Spectrometry (MS) Determines the mass-to-charge ratio of ionized protein fragments, providing information on protein composition, modifications, and interactions. Suitable for identifying post-translational modifications, characterizing protein-protein interactions, and conducting proteomics studies.
Fourier Transform Infrared Spectroscopy (FTIR) Measures the absorption of infrared light by proteins, providing information about secondary structure and conformational changes. Useful for studying protein folding, aggregation, and interactions with other molecules, often used in biophysical studies.
Dynamic Light Scattering (DLS) Measures the scattering of light by particles in solution to determine the size distribution and aggregation state of proteins. Ideal for analyzing protein aggregation, determining particle size distribution, and assessing sample quality before crystallization.
Fluorescence Spectroscopy Uses the emission of light by fluorescently labeled proteins to study their structure, dynamics, and interactions. Suitable for real-time analysis of protein interactions, conformational changes, and studying protein dynamics in solution.
Electron Paramagnetic Resonance (EPR) Spectroscopy Uses magnetic fields to study the electronic structure of paramagnetic centers in proteins, providing information about the local environment and dynamics. Ideal for studying metal-containing proteins, radical species, and conformational changes, often used in bioinorganic chemistry.

Each method for protein structure characterization offers unique advantages and is chosen based on the specific requirements of the study, such as the resolution needed, the state of the protein (crystalline or in solution), and the type of information sought. These techniques are essential tools in advancing our understanding of protein biology and developing new therapeutic strategies.

Service Process

The process of protein structure characterization involves several critical and interrelated steps:

  1. Project Consultation: Collaborating with researchers to define specific structural characterization requirements, including the target protein, desired resolution, and intended application.
  2. Protein Expression and Purification: Producing and purifying the target protein in a suitable expression system to ensure high purity and stability.
  3. Crystallization and Sample Preparation: Preparing protein samples for structural analysis, including crystallization for X-ray crystallography or grid preparation for cryo-EM.
  4. Data Collection: Collecting high-resolution data using techniques such as X-ray crystallography, NMR spectroscopy, or cryo-EM.
  5. Data Processing and Analysis: Processing and analyzing the collected data to determine the three-dimensional structure of the protein. This includes model building, refinement, and validation.
  6. Structural Interpretation: Interpreting the structural data to understand protein function, interactions, and mechanisms. Advanced computational tools are used for detailed analysis.
  7. Reporting and Consultation: Providing a detailed report of the findings and offering further consultation to interpret the results and plan subsequent research steps.

Examples and Solutions

The following table provides an overview of various case studies in protein structure characterization and the solutions we offer to support your research and biotechnological endeavors:

Case Study Description Solutions We Offer
Drug Target Structure Determination Determining the structure of a protein target to identify binding sites for drug design. Protein crystallization, X-ray crystallography, and structure analysis.
Enzyme Mechanism Elucidation Studying the structure of an enzyme to understand its catalytic mechanism. NMR spectroscopy, enzyme assays, and structural interpretation.
Protein-Protein Interaction Mapping Characterizing the interaction sites between proteins in a complex. Cryo-EM, cross-linking, and computational modeling.
Disease-Related Protein Structures Investigating the structural basis of disease-associated protein mutations. Crystallization, cryo-EM, and mutation analysis.
Industrial Enzyme Optimization Determining the structure of an industrial enzyme to improve its performance. X-ray crystallography, enzyme engineering, and activity assays.
Synthetic Biology Constructs Designing and characterizing proteins for synthetic biology applications. Protein design, structural modeling, and validation assays.

Frequently Asked Questions

Q: What is protein structure characterization?

A: Protein structure characterization involves determining the three-dimensional arrangement of atoms within a protein. This information is crucial for understanding protein function, interactions, and mechanisms of action.

Q: How is protein structure characterization performed?

A: Protein structure characterization is performed through a series of steps including project consultation, protein expression and purification, crystallization and sample preparation, data collection, data processing and analysis, structural interpretation, and reporting. Each step ensures accurate and high-resolution structural data.

Q: What are the applications of protein structure characterization?

A: Applications include drug discovery, enzyme engineering, structural biology, disease research, biotechnology, and protein-protein interaction studies. Characterizing protein structures provides essential insights for various research and biotechnological applications.

Q: What are the key steps in the protein structure characterization process?

A: Key steps include project consultation, protein expression and purification, crystallization and sample preparation, data collection, data processing and analysis, structural interpretation, and reporting. These steps ensure comprehensive and accurate analysis of protein structures.

Q: Why is protein structure characterization important?

A: Protein structure characterization is important for advancing research, developing new therapies, designing novel enzymes, and understanding disease mechanisms. Detailed structural insights enable precise and targeted interventions in biological processes.

For more information about our Protein Structure Characterization Services or to discuss your specific needs, please contact us. Our team of experts is available to provide guidance and support for your research and biotechnological projects, ensuring you achieve your scientific and industrial goals.

Please note that all services are for research use only. Not intended for any clinical use.

Get a free quote

If your question is not addressed through these resources, you can fill out the online form below and we will answer your question as soon as possible.


There is no product in your cart.