PY - 2006/3/1. Protein (0.15 mg/mL) in 200 mM sodium phosphate buffer (pH 7.0) was subjected to heat-induced denaturation. Silica gels have demonstrated the ability to retain protein structure and functionality. Signals were monitored at 223 nm on a 202SF CD spectrometer (AVIV), equipped with a Peltier temperature controller.

where T m is the melting temperature of the protein, and ΔH 0 m and are the standard folding enthalpy at T m and the change in heat capacity upon folding, respectively.

Proteins from thermophilic (growth temperature ∼ 45–75 °C) and hyperthermophilic (growth temperature ≥ 80 °C) organisms exhibit remarkable thermal stability and resistance to chemical denaturants [[1-3]].Despite decades of research in this field, a general concept for how this stability is achieved remains elusive. Here, we used quantitative mass spectrometry to systematically analyze the thermal stability and solubility of proteins on a proteome-wide scale during the eukaryotic cell cycle.

Y1 - 2006/3/1. Thermal shift analysis of protein stability and ligand interactions.

Introduction. (A) Starting with a purified recombinant protein in its native (folded) state, the protein is slowly heated to undergo thermal denaturation.The environmentally sensitive dye, SYPRO Orange, interacts with hydrophobic regions in the protein that become exposed upon denaturation.
For example, thermophiles and hyperthermophiles, kinds of extremophile, can live in high‐temperature environments (≈120 °C at most) such as hot springs and deep sea hydrothermal vents owing to the thermal stability of their constitutive proteins.

Various cellular pathways and components vary in thermal stability, such as cell-cycle factors, polymerases, and chromatin remodelers. Amino acid composition and thermal stability of proteins. Animal feed is comprised of an ingredient mixture that provides nutrition and promotes the health of pets and livestock. Yet, less thermostable proteins possess a … International Journal of Biological Macromolecules 1982, 4 (3) , 186-190. Proteins from thermophilic (growth temperature ∼ 45–75 °C) and hyperthermophilic (growth temperature ≥ 80 °C) organisms exhibit remarkable thermal stability and resistance to chemical denaturants [[1-3]].Despite decades of research in this field, a general concept for how this stability is achieved remains elusive. The protein’s melting temperature (Tm) is a reporter of the protein’s thermal stability.

AU - Bischof, John C. AU - He, Xiaoming. @article{osti_22594259, title = {The role of stabilization centers in protein thermal stability}, author = {Magyar, Csaba and Gromiha, M. Michael and Sávoly, Zoltán and Simon, István}, abstractNote = {The definition of stabilization centers was introduced almost two decades ago.

T1 - Thermal stability of proteins. Applications • Optimize buffer formulation for protein stability and storage • Determine how mutations affect your protein’s stability • Rapidly screen small molecule drug candidates and other ligands for protein binding Cat.
We demonstrate that protein thermal stability serves as a proxy for enzyme activity, DNA binding, and complex formation in situ.

Our data show a clear direct relationship between protein thermal stability and intracellular abundance and an inverse relationship between protein stability and aggregation or local unfolding.


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