BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions

Nikolić, Mina; Brudar, Sandi; Coutsias, Evangelos A.; Dill, Ken A.; Lukšič, Miha; Simmerling, Carlos; Hribar-Lee, Barbara

doi:10.3390/ijms232315371

Cited by 2 publications

(1 citation statement)

References 17 publications

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“…We begin by presenting the results for the experimentally measured phase stability of the HEWL solutions in the presence of free arginine molecules. It was established that the formation of protein aggregates in the solution leads to a liquid–liquid phase separation which can be detected by measuring the

of protein solutions [ 16 , 17 ]. Because it was shown before that different concentrations of arginine molecules can affect the stability of protein solutions through a different mechanism [ 8 ], we here determined how the

of HEWL solutions depends on the arginine concentration.…”

Section: Results and Discussionmentioning

confidence: 99%

The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions

Brudar

Hribar-Lee

2023

IJMS

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The effect of arginine on the phase stability of the hen egg-white lysozyme (HEWL) has been studied via molecular dynamics computer simulations, as well as experimentally via cloud-point temperature determination. The experiments show that the addition of arginine increases the stability of the HEWL solutions. The computer simulation results indicate that arginine molecules tend to self-associate. If arginine residues are located on the protein surface, the free arginine molecules stay in their vicinity and prevent the way protein molecules “connect” through them to form clusters. The results are not sensitive to a particular force field and suggest a possible microscopic mechanism of the stabilizing role of arginine as an excipient.

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of HEWL solutions depends on the arginine concentration.…”

Section: Results and Discussionmentioning

confidence: 99%

The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions

Brudar

Hribar-Lee

2023

IJMS

Self Cite

View full text Add to dashboard Cite

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Biophysical Principles Emerging from Experiments on Protein–Protein Association and Aggregation

Hribar-Lee,

Lukšič

2024

Annual Review of Biophysics

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Protein–protein association and aggregation are fundamental processes that play critical roles in various biological phenomena, from cellular signaling to disease progression. Understanding the underlying biophysical principles governing these processes is crucial for elucidating their mechanisms and developing strategies for therapeutic intervention. In this review, we provide an overview of recent experimental studies focused on protein–protein association and aggregation. We explore the key biophysical factors that influence these processes, including protein structure, conformational dynamics, and intermolecular interactions. We discuss the effects of environmental conditions such as temperature, pH and related buffer-specific effects, and ionic strength and related ion-specific effects on protein aggregation. The effects of polymer crowders and sugars are also addressed. We list the techniques used to study aggregation. We analyze emerging trends and challenges in the field, including the development of computational models and the integration of multidisciplinary approaches for a comprehensive understanding of protein–protein association and aggregation. Expected final online publication date for the Annual Review of Biophysics, Volume 53 is May 2024. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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BioMThermDB 1.0: Thermophysical Database of Proteins in Solutions

Cited by 2 publications

References 17 publications

The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions

The Effect of Arginine on the Phase Stability of Aqueous Hen Egg-White Lysozyme Solutions

Biophysical Principles Emerging from Experiments on Protein–Protein Association and Aggregation

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