Proteins and other biomolecules are inherently sensitive structures. Their size, conformation, and interactions can shift significantly depending on their surroundings. Factors such as temperature, ionic strength, labeling, or immobilization to a surface may alter their native state. When molecules are forced into non-physiological conditions, the data obtained may no longer reflect their true behavior.

Analysing directly in-solution avoids many of these distortions, preserving the molecules in an environment closer to their natural physiological state.

Benefits of In-Solution Analysis

1. Mimicking Physiological Conditions

In-solution studies provide data that are more representative of the environment in which proteins and particles actually function. This reduces artefacts caused by surface binding or chemical modifications.

2. Capturing Molecular Dynamics

Many biological processes depend on dynamic, reversible interactions. In-solution approaches allow observation of conformational changes, binding equilibria, and molecular assemblies as they naturally occur, offering a more complete understanding than static measurements.

3. Improving Data Reliability

Because in-solution methods avoid external perturbations such as immobilization or labeling, they generally produce data of higher reliability. This is critical for experiments where subtle differences in affinity, stability, or aggregation can change conclusions.

4. Supporting Broad Applications

Accurate in-solution insights are valuable across fields such as:

Drug discovery: better prediction of therapeutic efficacy.
Diagnostics: improved understanding of biomarker behavior.
Biotechnology: optimisation of protein engineering and formulation.

Conclusion

Analysing biomolecules in-solution ensures that experimental data reflect true molecular properties and interactions. By studying proteins and particles in a near-native environment, researchers can achieve more reliable, physiologically relevant insights — ultimately strengthening both fundamental research and applied development.

You might also be interested in publications/application notes below:

In-solution Characterization of Biomolecular Interaction Kinetics under Native Conditions

Flow Induced Dispersion Analysis Rapidly Quantifies Proteins in Human Plasma Samples

A serum-stable RNA aptamer specific for SARS-CoV-2 neutralizes viral entry

Continuous Titration Based Method for Rapid In-Solution Analysis of Non-Covalent Interactions

Screening de. novo designed protein binders in unpurified lysate using flow induced dispersion analysis

Degree of hydrolysis is a poor predictor of the sensitizing capacity of whey- and casein-based hydrolysates in a Brown Norway rat model of cow’s milk allergy

Correlating Supramolecular Behaviour in Buffer and Plasma

Protein Oligomerization: Easy and Accurate determination in plasma and buffer

HLA antibody affinity determination: From HLA-specific monoclonal antibodies to donor HLA specific antibodies (DSA) in patient serum

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