Increasing the temperature by just a few degrees may lead to structural perturbation or
unfolding of the protein and consequent loss of function. The concepts of flexibility and …

Faced with desiccation stress, many organisms deploy strategies to maintain the integrity of
their cellular components. Amorphous glassy media composed of small molecular solutes or …

Solutes added to buffered solutions directly impact protein folding. Protein stabilization by
cosolutes or crowders has been shown to be largely driven by protein–cosolute volume …

Sensitive in-cell distance measurements in proteins using pulsed-electron spin resonance
(ESR) require reduction-resistant and cleavage-resistant spin labels. Among the reduction …

The recurrence and metastasis of colorectal cancer (CRC) have been considered as a
severe challenge in clinical treatment. Recent studies have demonstrated that matrix …

Protein denaturation in concentrated solutions consists of the unfolding of the native protein
structure, and subsequent cross-linking into clusters or gel networks. While the kinetic …

TREX1 is a cytosolic DNA nuclease essential for regulation of cGAS-STING immune
signaling. Existing structures of mouse TREX1 establish a mechanism of DNA degradation …

Thermal stability is one of the most important properties of enzymes, which sustains life and
determines the potential for the industrial application of biocatalysts. Although traditional …

α-N-Methylation (Nα-methylation), catalyzed by protein N-terminal methyltransferases
(NTMTs), constitutes a crucial post-translational modification involving the transfer of a …

In lens, αβγ-crystallins accounting for∼ 90% of ocular proteins with concentrations> 400
mg/ml need to remain soluble for the whole life-span and their aggregation can lead to …