As proteins typically have charges of around 10, they will interact strongly with charged surfaces. We calculate the electrostatic contribution to the interaction of crystals of protein with charged surfaces. The surfaces repel like-charged crystals and attract oppositely-charged crystals, with free energies which can be easily several kT per protein molecule brought into contact with the surface. This means that oppositely charged surfaces can act as a nucleant, they can induce nucleation of a protein crystal by lowering the free energy barrier to heterogeneous nucleation of the crystal from a dilute solution
Analysis of known protein crystal structures reveals that interaction energies between monomer pairs...
Nucleation is the rate-limiting step in protein crystallization. Introducing heterogeneous substrate...
Protein crystallization can function as an effective method for protein purification or formulation....
Functionalized mica sheets and polystyrene films exposing ionisable groups have been used as heterog...
The synthesis of high quality protein crystals is essential for determining their structure. Hence t...
The most powerful method for protein structure determination is X-ray crystallography which relies o...
Homogeneous nucleation of protein crystals in solution is tackled from both thermodynamic and energe...
We use a coarse-grained model for generic proteins to investigate the formation of structures with P...
Protein crystallization is an essential step, and often a bottleneck, in the structure determination...
In this paper we report calculations of the concentration profile and the Gibbs free energy of the i...
The mechanisms of electrostatically driven adsorption of proteins on charged surfaces are studied wi...
The interactions of proteins with surfaces are important in both biological processes and biotechnol...
Physical and biochemical aspects of protein crystal nucleation can be distinguished in an appropriat...
Interactions of proteins with other proteins, with polymers and with surfaces are of great practical...
Electrostatic interactions in bio-molecular systems are important not only in the living cell but al...
Analysis of known protein crystal structures reveals that interaction energies between monomer pairs...
Nucleation is the rate-limiting step in protein crystallization. Introducing heterogeneous substrate...
Protein crystallization can function as an effective method for protein purification or formulation....
Functionalized mica sheets and polystyrene films exposing ionisable groups have been used as heterog...
The synthesis of high quality protein crystals is essential for determining their structure. Hence t...
The most powerful method for protein structure determination is X-ray crystallography which relies o...
Homogeneous nucleation of protein crystals in solution is tackled from both thermodynamic and energe...
We use a coarse-grained model for generic proteins to investigate the formation of structures with P...
Protein crystallization is an essential step, and often a bottleneck, in the structure determination...
In this paper we report calculations of the concentration profile and the Gibbs free energy of the i...
The mechanisms of electrostatically driven adsorption of proteins on charged surfaces are studied wi...
The interactions of proteins with surfaces are important in both biological processes and biotechnol...
Physical and biochemical aspects of protein crystal nucleation can be distinguished in an appropriat...
Interactions of proteins with other proteins, with polymers and with surfaces are of great practical...
Electrostatic interactions in bio-molecular systems are important not only in the living cell but al...
Analysis of known protein crystal structures reveals that interaction energies between monomer pairs...
Nucleation is the rate-limiting step in protein crystallization. Introducing heterogeneous substrate...
Protein crystallization can function as an effective method for protein purification or formulation....