Dissociation of cytosolic complex leads to the stabilization of the full-length Ci, which moves into the

nucleus, displaces the repressor Ci75 from the promoter of target genes, and induces expression of target genes.

TLS Online TPP Program

#Id: 8442

#XL - T Zoology

The proportion of occupied patches will stabilize over time to =1− (x/m)

x - Extinction rate 

m - Rate of movement between patches

TLS Online TPP Program

#Id: 4333

#XL - T Zoology

About 75% of the charged residues in proteins are members of ion pairs that are located mostly on the protein surface.

Despite the strong electrostatic attraction interactions contribute little to the stability of a native protein.

TLS Online TPP Program

#Id: 4356

#XL - T Zoology

The overall probability of RNase A re-forming its four native disulfide links at random is-

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.