Liquid-liquid phase separation (LLPS) is an important phenomenon in soft condensed matter that explains many properties of membraneless organelles in living cells. The research on this topic is, therefore, a field with a wide range of applications such as biopharmacy and biomaterials. In this project, we investigate the LLPS of the antibody protein Immunoglobulin G (IgG) by analyzing the liquid dynamics of IgG solutions at a wide range of temperatures with dynamic light scattering (DLS). It was found that the slow component of the autocorrelation function increases with decreasing temperature below 0 °C. This can be attributed to either the number of protein clusters increasing as the sample approaches phase separation or LLPS droplets form...
Cryoglobulins are proteins that precipitate at temperatures below 37 degreesC. Coldinduced precipita...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
We study the kinetics of the liquid–liquid phase separation (LLPS) and its arrest in protein solutio...
The liquid-liquid phase separation (LLPS) of biomolecules is a phenomenon which received a lot of at...
We report the observation of liquid-liquid phase separation in a solution of human monoclonal antibo...
Antibodies are a fundamental part of the immune system. They are injected subcutaneously to treat di...
Phase transformation in antibody solutions is of growing interest in both academia and the pharmaceu...
A common observation by protein chemists has been the appearance, for many proteins in aqueous solut...
Liquid–liquid phase separation (LLPS) of monoclonal antibody (mAb) formulations involves spontaneous...
The crystallization of Anti-CD20, a full-length monoclonal antibody, has been studied in the PEG400/...
The broad objective of my research is to investigate the physical characteristics and interactions o...
Phase transformation in antibody solutions is of growing interest in both academia and the ...
Colloidal stability of antibody solutions, i.e., the propensity of the folded protein to precipitate...
We report our use of static and dynamic light scattering techniques to study aqueous solutions of th...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
Cryoglobulins are proteins that precipitate at temperatures below 37 degreesC. Coldinduced precipita...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
We study the kinetics of the liquid–liquid phase separation (LLPS) and its arrest in protein solutio...
The liquid-liquid phase separation (LLPS) of biomolecules is a phenomenon which received a lot of at...
We report the observation of liquid-liquid phase separation in a solution of human monoclonal antibo...
Antibodies are a fundamental part of the immune system. They are injected subcutaneously to treat di...
Phase transformation in antibody solutions is of growing interest in both academia and the pharmaceu...
A common observation by protein chemists has been the appearance, for many proteins in aqueous solut...
Liquid–liquid phase separation (LLPS) of monoclonal antibody (mAb) formulations involves spontaneous...
The crystallization of Anti-CD20, a full-length monoclonal antibody, has been studied in the PEG400/...
The broad objective of my research is to investigate the physical characteristics and interactions o...
Phase transformation in antibody solutions is of growing interest in both academia and the ...
Colloidal stability of antibody solutions, i.e., the propensity of the folded protein to precipitate...
We report our use of static and dynamic light scattering techniques to study aqueous solutions of th...
Liquid–liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
Cryoglobulins are proteins that precipitate at temperatures below 37 degreesC. Coldinduced precipita...
Liquid-liquid phase separation (LLPS) in protein systems is relevant for many phenomena, from protei...
We study the kinetics of the liquid–liquid phase separation (LLPS) and its arrest in protein solutio...