Advances in protein solubility and thermodynamics: quantification, instrumentation, and perspectives

Ferreira, Joana; Castro, Filipa

doi:10.1039/d3ce00757j

Cited by 2 publications

(2 citation statements)

References 127 publications

(226 reference statements)

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“…170,217 Many reviews have already reported the advantages and possible applications of microfluidics to study proteins at different levels, including thermodynamic parameters 218 and their solubility and crystallization. 219,220 5.4. Protein Crystallization: Between Evolution and Applicability.…”

Section: Crystallization Methods and Facilities Aim To Eliminate Natu...mentioning

confidence: 99%

“…This is because microfluidics enables the realization of the same experimental setups on a single chip (Lap-on-a-Chip) at a much smaller scale (per experimental hit) with higher mixing and thus heat transfer efficiencies and lower energy consumption, combining the benefits of the capillarity effect and, if intended, gel-mediated crystallization. , Applying microfluidics for protein crystallization offers essentially a high-throughput platform to systematically screen different solution combinations (protein + buffer + precipitant + additive) simultaneously. ,, Additionally, microfluidic devices have been designed to facilitate in situ data collection . Nowadays, microfluidics technology has been exploited to allow for the application of other well-established crystallization methods such as dialysis and counter-diffusion. , Many reviews have already reported the advantages and possible applications of microfluidics to study proteins at different levels, including thermodynamic parameters and their solubility and crystallization. , …”

Section: Protein Crystal Growth: Methodologies and Kineticsmentioning

confidence: 99%

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A Tutorial Review on the Methodologies and Theories Utilized to Handle Proteins toward Obtaining Single Protein Crystals

Adawy

2024

Crystal Growth & Design

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Proteins are functional macromolecules in living organisms including mammals and thus human beings. They are involved in almost all biological processes, either as the main functional domains or as catalysts (enzymes). Owing to their vitality, proteins have attracted extensive research interest from different structural perspectives. Precise determination of the three-dimensional structures of proteins is crucial; otherwise, the structure−function relationships would be ambiguous. Macromolecular crystallographers have been trying to determine protein structures since the 1950s. According to the protein data bank (PDB) on February 13, 2024, 215 684 structures of proteins, nucleic acids, and other biological macromolecules have been determined. Most of these structures (84.6%) were solved using Xray diffraction (XRD), which requires the growth of protein microcrystals. Only 0.108% and 0.104% of all structures were solved using electron and neutron crystallography methods, which require the growth of nanocrystals and mesoscopic crystals, respectively. Other methodologies such as nuclear magnetic resonance (NMR) (6.5%), electron microscopy (EM) (8.5%), and other biochemical methodologies (<1%) have contributed to solving the remaining structures. This implies the necessity of growing protein crystals, for which prior procedures are required. This tutorial Review covers the structural aspects and some of the methodologies and theories used on the route to obtaining the starting purified protein sample that would later be induced to assemble into functional assemblies up to protein crystals to reveal the structure−function relationship of these entities through the usage of biochemical methods and eventually macromolecular crystallography. In particular, this Review touches on the procedures used to purify proteins and to crystallize them, with a special mention of the recent efforts reported for understanding of the actual mechanism behind protein nucleation, crystal growth, the incorporation of impurities, and the methods developed to facilitate the crystallization of proteins into high-quality crystals: processes widely known as the bottleneck in the determination of the macromolecular structures of proteins using state-of-art macromolecular crystallography methodologies that rather made the process, after crystal obtention, quite straightforward.

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Section: Crystallization Methods and Facilities Aim To Eliminate Natu...mentioning

confidence: 99%

Section: Protein Crystal Growth: Methodologies and Kineticsmentioning

confidence: 99%

A Tutorial Review on the Methodologies and Theories Utilized to Handle Proteins toward Obtaining Single Protein Crystals

Adawy

2024

Crystal Growth & Design

View full text Add to dashboard Cite

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Plant protein solubility: A challenge or insurmountable obstacle

Gao,

Rao,

Chen

2024

Advances in Colloid and Interface Science

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Advances in protein solubility and thermodynamics: quantification, instrumentation, and perspectives

Abstract: While protein crystallization has broadly been applied to determine the 3D structure of proteins, it has recently drawn great attention to replace the traditional downstream processing for protein-based biopharmaceuticals due...

Cited by 2 publications

References 127 publications

A Tutorial Review on the Methodologies and Theories Utilized to Handle Proteins toward Obtaining Single Protein Crystals

A Tutorial Review on the Methodologies and Theories Utilized to Handle Proteins toward Obtaining Single Protein Crystals

Plant protein solubility: A challenge or insurmountable obstacle

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