Mutation and natural selection act as opposing forces on detrimental alleles.

TLS Online TPP Program

#Id: 4385

#XL - T Zoology

Proteins fold to their native conformations via directed pathways rather than stumbling on them through random conformational searches.

TLS Online TPP Program

#Id: 8749

#XL - T Zoology

Intrinsically disordered proteins lack a hydrophobic core, and have high densities of charged amino acid residues such as Lys, Arg, and Glu. Pro residues are also prominent, as they tend to disrupt ordered structures.

TLS Online TPP Program

#Id: 8750

#XL - T Zoology

The lack of an ordered structure can facilitate a kind of functional promiscuity, allowing one protein to interact with multiple partners. Some intrinsically disordered proteins act to inhibit the action of other proteins by an unusual mechanism: wrapping around their protein targets.

TLS Online TPP Program

#Id: 8751

#XL - T Zoology

The protein p27 is intrinsically disordered. It wraps around and inhibits the action of several enzymes called protein kinases that facilitate cell division. 

TLS Online TPP Program

#Id: 8752

#XL - T Zoology

Predictor of Natural Disordered Regions or PONDR is one of the best available algorithms for predicting the likelihood that a given amino acid residue is in a region of intrinsic disorder, based on the surrounding amino acid sequence and amino acid composition. 

TLS Online TPP Program

#Id: 8753

#XL - T Zoology

A PONDR score of 1.0 indicates a probability of 100% that a protein will be disordered.