Publications by authors named "M Luksic"

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.

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In all biologically relevant media, proteins interact in the presence of surrounding ions, and such interactions are water-mediated. Water molecules play a crucial role in the restructuring of proteins in solution and indeed in their biological activity. Surface water dynamics and proton exchange at protein surfaces is investigated here using NMR relaxometry, for two well-known globular proteins, lysozyme and bovine serum albumin, with particular attention to the role of surface ions.

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Prediction of analyte retention times requires prior knowledge of the column void volume, the measurement of which is still highly contested within the literature and therefore experimental based prediction is often used. In this study, we investigated deuterated acetonitrile as an isotopically labelled mobile phase component to observe its elution behaviour in a binary mixture with water at 25 different mobile phase compositions (from 5 to 95 vol.% of acetonitrile), on two stationary phases (C8 and C18), and at two temperatures (30 and 40 °C) using LC-MS.

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Most organic solvents are colorless liquids, usually stored in sealed containers. In many cases, their identification depends on the appropriate description on the container to prevent mishandling or mixing with other materials. Although modern laboratories rely heavily on identification technologies, such as digitized inventories and spectroscopic methods (e.

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Article Synopsis
  • BioMThermDB 1.0 is a free web-based database that provides thermophysical and dynamic properties of proteins and their solutions.
  • It includes detailed information such as hydrodynamic radius, electrophoretic mobility, and other key properties, along with the experimental conditions and methods used to determine them.
  • The database supports meta-analysis and data visualization, helping researchers compare findings and align theoretical predictions with experimental results.
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