Prenucleation, crystal growth and polymorphism of some proteins

Veesler, Stéphane; Lafont, Sylvaine; Marcq, Sylvie; Astier, Jean-Pierre; Boistelle, R.

doi:10.1016/0022-0248(96)00373-9

Cited by 32 publications

(31 citation statements)

References 15 publications

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“…37,48 The light scattering experimental setup (SEM 633, SematechFrance) has previously been described elsewhere. 49 The appearance of liquid droplets when temperature was decreased induced a jump in the scattering intensity, designated as T L-L . After the L-L phase demixion had occurred, when temperature was increased above T L-L , the cloudiness responsible for the strong signal peak readily disappeared.…”

Section: (C T)mentioning

confidence: 99%

“…3 Protein phase separations can also be the cause of human diseases, such as cataract 4 or sickle cell disease. 5 Despite their fundamental importance, phase diagrams of only a few proteins have been studied: insulin, 6 fibrinogen, 7 γ-crystallin, 8 lysozyme, 4,9-12 concanavalin, 13 canavalin, 14 R-amylase, 15,16 collagenase, 17 bovine pancreatic trypsin inhibitor (BPTI), 16,18 apoferritin, 19 endoglucanase A, 20 and the photochemical reaction center from Rhodobacter sphaeroides Y. 21 Recently, there has been a renewed enthusiasm for phasetransition studies of colloids 22 and proteins [22][23][24][25][26][27] due to advances in experimental and computational technologies.…”

Section: Introductionmentioning

confidence: 99%

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Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

et al. 2006

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This paper presents an investigation of the phase diagram of BPTI (bovine pancreatic trypsin inhibitor)/350 mM KSCN at pH 4.9 by direct observation and numerical simulations. We report optical microscopy and light and X-ray scattering experiments coupled with theoretical data analysis using numerical tools. The phase diagram is thoroughly determined, as a function of temperature. Two polymorphs are observed by video microscopy and their solubility measured. In this phase diagram, the liquid-liquid phase separation (LLPS) is metastable with respect to the solid-liquid phase separation. Above the T L-L boundary curve, solutions are composed of a mixture of BPTI monomers and decamers. Attractive interactions are stronger between decamers than between monomers. Below the T L-L boundary curve, the dense phase is highly concentrated in protein and composed of BPTI decamers alone. Thus, the driving force for liquid-liquid or liquid-solid phase separation is the attraction between decamers at low pH. The structure factors of the dense phases are characteristic of repulsive dense phases because of a hard sphere repulsion core, meaning that in the dense phase proteins are actually in contact (interparticle distance of 53 Å). In agreement with the Oswald rule of stages, LLPS occurs prior to and impedes the solid nucleation.

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Section: (C T)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

et al. 2006

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“…The crystals under consideration are different polymorphs of porcine pancreatic -amylase (Boistelle et al, 1992;Veesler et al, 1994), bovine pancreatic trypsin inhibitor (BPTI) and different ®sh parvalbumins (Lafont, 1996). Since we have previously established their phase diagrams and the crystallization conditions, we decided to ®rst carry out experiments with these proteins, together with chicken eggwhite lysozyme which is easily available and also the protein most studied by crystal growers.…”

Section: Proteinsmentioning

confidence: 99%

Protein crystals orientation in a magnetic field

1998

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Nucleation and crystal growth of hen egg-white lysozyme, bovine pancreatic trypsin inhibitor and porcine pancreatic -amylase were carried out in the presence of a magnetic ®eld of 1.25 T produced by small permanent magnets. Crystals were oriented in the magnetic ®eld, except when heterogeneous nucleation occurred. The orientation of protein crystals in the presence of a magnetic ®eld can be attributed to the anisotropic diamagnetic susceptibility of proteins resulting from the large anisotropy of the -helices due to the axial alignment of the peptide bonds.

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“…There is also a correlation between the solubility of a protein in an electrolyte solution and the osmotic second virial coefficient B 2 of the solution (Veesler et al [2], Boistelle et al [3]). These observations have led to numerous studies on the second virial coefficients of protein solutions with the hope to use this property to narrow down the parameter space of protein solutions for the search of optimal crystallization conditions.…”

Section: Introductionmentioning

confidence: 99%

Calculations of the second virial coefficients of protein solutions with an extended fast multipole method

Kim

Song

2011

Phys. Rev. E

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The osmotic second virial coefficients B2 are directly related to the solubility of protein molecules in electrolyte solutions and can be useful to narrow down the search parameter space of protein crystallization conditions. Using a residue level model of protein-protein interaction in electrolyte solutions B2 of bovine pancreatic trypsin inhibitor and lysozyme in various solution conditions such as salt concentration, pH and temperature are calculated using an extended fast multipole method in combination with the boundary element formulation. Overall, the calculated B2 are well correlated with the experimental observations for various solution conditions. In combination with our previous work on the binding affinity calculations it is reasonable to expect that our residue level model can be used as a reliable model to describe protein-protein interaction in solutions. Disciplines Chemistry CommentsThis article is from Physical Review E 83 (2011) The osmotic second virial coefficients B 2 are directly related to the solubility of protein molecules in electrolyte solutions and can be useful to narrow down the search parameter space of protein crystallization conditions. Using a residue level model of protein-protein interaction in electrolyte solutions B 2 of bovine pancreatic trypsin inhibitor and lysozyme in various solution conditions such as salt concentration, pH and temperature are calculated using an extended fast multipole method in combination with the boundary element formulation. Overall, the calculated B 2 are well correlated with the experimental observations for various solution conditions. In combination with our previous work on the binding affinity calculations it is reasonable to expect that our residue level model can be used as a reliable model to describe protein-protein interaction in solutions.

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Prenucleation, crystal growth and polymorphism of some proteins

Cited by 32 publications

References 15 publications

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

Exploring Bovine Pancreatic Trypsin Inhibitor Phase Transitions

Protein crystals orientation in a magnetic field

Calculations of the second virial coefficients of protein solutions with an extended fast multipole method

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