MEK, a dual-specificity protein kinase

TLS Online TPP Program

#Id: 8762

#XL - T Zoology

Thermostable proteins have such a high incidence of salt bridges.

TLS Online TPP Program

#Id: 8763

#XL - T Zoology

Thermophilic proteins have increased amounts of Arg, increased occurrence of Ala in helices, and Gly/Ala substitutions (which affect the entropy of the denatured state, and thus its free energy) and increased number of salt bridges. 

TLS Online TPP Program

#Id: 8764

#XL - T Zoology

Some thermostable proteins are stabilized by an increased size of the protein’s hydrophobic core, an increased size of the interface between its domains and/or subunits, and a more tightly packed core as evidenced by a reduced surface-to-volume ratio.

TLS Online TPP Program

#Id: 8765

#XL - T Zoology

Disulfide bonds are believed to increase the stability of the native state by decreasing the conformational entropy of the unfolded state due to the conformational constraints imposed by cross-linking (i. e. decreasing the free energy of the unfolded state).  

TLS Online TPP Program

#Id: 8766

#XL - T Zoology

Most protein have "loops" introduced by disulfides of about 15 residues

TLS Online TPP Program

#Id: 8767

#XL - T Zoology

Guanidinium ion and urea are chaotropic agents which disrupts hydrophobic core of proteins.