2019
DOI: 10.1021/acs.jpcb.9b07774
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Using Schematic Models to Understand the Microscopic Basis for Inverted Solubility in γD-Crystallin

Abstract: Inverted solubility-a crystal melting upon cooling-is observed in a handful of proteins, such as carbomonoxy hemoglobin and γD-crystallin. In human γD-crystallin, the phenomenon is associated with the mutation of the 23 rd residue, a proline, to a threonine, serine or valine. One proposed microscopic mechanism for this effect entails an increase in hydrophobicity upon mutagenesis. Recent crystal structures of a double mutant that includes the P23T mutation allows for a more careful investigation of this propos… Show more

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Cited by 5 publications
(5 citation statements)
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“…For instance, patchy sphere models represent an entire protein as a single sphere, with “patches” on the sphere surface that have unique interactions properties . Patchy particles have been used for simulating self-assembly, , as well as protein phase behavior such as in the case of γ-Dc. …”
Section: Introductionmentioning
confidence: 99%
“…For instance, patchy sphere models represent an entire protein as a single sphere, with “patches” on the sphere surface that have unique interactions properties . Patchy particles have been used for simulating self-assembly, , as well as protein phase behavior such as in the case of γ-Dc. …”
Section: Introductionmentioning
confidence: 99%
“…Nevertheless, the so‐called patchy colloid models lack the molecular‐level detail necessary to be predictive for specific systems. Patch interactions can be parameterized using specific contact information from crystallographic structures and additional potential of mean force calculations from atomistic molecular dynamics (MD) simulations 3–5 . Here, we use a recently developed approach to many‐protein atomistic simulations 6 to directly sample protein–protein interactions under experimentally relevant conditions.…”
Section: Introductionmentioning
confidence: 99%
“…Patch interactions can be parameterized using specific contact information from crystallographic structures and additional potential of mean force calculations from atomistic molecular dynamics (MD) simulations. [3][4][5] Here, we use a recently developed approach to many-protein atomistic simulations 6 to directly sample protein-protein interactions under experimentally relevant conditions. This approach has the potential to bridge the gap between information on individual-proteins and highly coarse-grained levels of description.…”
mentioning
confidence: 99%
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“…16,17 The patchy colloid framework can also more generally recapitulate the phase behaviors of globular proteins like S-crystallins. [18][19][20][21][22][23][24] The temperature-packing fraction (T-f) phase diagram of patchy particles includes a binodal, below which the system undergoes liquid-liquid phase separation, a percolation line, below which patchy particles tend to form volume-spanning networks (i.e. gels), and possibly a glass transition line (Fig.…”
Section: Introductionmentioning
confidence: 99%