Explore: Intrinsically Disordered Proteins

PMID 30430826. Oldfield CJ, Dunker AK (2014). "Intrinsically disordered proteins and intrinsically disordered protein regions". Annual Review of Biochemistry

including freezing and desiccation. Research has shown that intrinsically disordered proteins in these organisms may work to stabilize cell function and

20–30% of all genes in most genomes encode membrane proteins. Intrinsically disordered proteins lack a fixed or ordered three-dimensional structure.

function of the flexible protein, extending the structure-function paradigm from folded proteins to intrinsically disordered proteins. The calculation of ensembles

Tardigrade specific proteins are types of intrinsically disordered proteins specific to tardigrades. These proteins help tardigrades survive desiccation

has its strengths and weaknesses but they all struggle with intrinsically disordered proteins without any clearly defined tertiary structure as the essence

the less stable variants are intrinsically disordered proteins. These proteins exist and function in a relatively 'disordered' state lacking a stable tertiary

unfolded" or intrinsically disordered proteins, characterized by high flexibility and a lack of ordered tertiary structure. These disordered proteins, referred

"Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation". Protein Science. 26 (4). Wiley: 718–726. doi:10

trehalose for this function. Instead, tardigrades produce intrinsically disordered proteins in response to desiccation. Three of these are specific to