Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Proteins recognition and binding

Roise, D. (1997). Recognition and binding of mitochondrial presequences during the import of proteins into mitochondria. / Bioenerg. Biomembr. 29, 19-27. [Pg.341]

Molecular recognition and binding is the first step in protein electron-electron transfer. The foregoing data suggests that for the prototypical cyt c ccp system, this binding does not involve specific lock and key recognition, but rather involves complementary sticky patches of protein surfaces (rather like two pieces of velcro adhesive). [Pg.173]

As only the 26S holoenzyme, but not the 20S-base complex degrades ubiquitylated proteins (Glickman et al. 1998a Thrower et al. 2000), it appears that recognition, and binding of ubiquitin-tagged substrates is mediated by the eight subunits of the lid subcomplex. [Pg.73]

The insulin receptor is composed of two heterodimers each heterodimer is composed of an a unit and a P unit. The a unit is extracellular and contains the insulin recognition and binding sites the p unit spans the cellular membrane and contains a tyrosine kinase. Although insulin can bind to a single ap dimer, it binds with higher affinity to the aPaP tetrameric complex. When insulin binds to an a unit, the tyrosine kinase associated with the corresponding p unit is stimulated. Following this, intracellular proteins such as IRS-1 and IRS-2 (IRS=insulin receptor substrate) are phosphorylated by the P subunit tyrosine kinase, and they in turn activate a network of phosphorylations within the receptor cell. [Pg.365]

Fig. 1.18. Structure and symmetry of DNA recognition elements and the ohgomeric structure of DNA-binding proteins, sequence and binding protein plays an important role in the specific binding process. If, for example, a mutation inactivates one half of the recognition sequence, the other intact site often no longer suffices to provide for a tight binding. The protein can then only bind weakly and the mutated DNA element is often inactive in the in vivo situation. Fig. 1.18. Structure and symmetry of DNA recognition elements and the ohgomeric structure of DNA-binding proteins, sequence and binding protein plays an important role in the specific binding process. If, for example, a mutation inactivates one half of the recognition sequence, the other intact site often no longer suffices to provide for a tight binding. The protein can then only bind weakly and the mutated DNA element is often inactive in the in vivo situation.
The bicyclic azacarbapenams 164 and 165 lack the carboxyl group critical for the recognition and binding between the /3-lactam group and the receptor protein. Therefore, a new synthetic strategy was developed from diazetidinone 166 as shown in Scheme 22 <1998J(P1)2597>. [Pg.663]

The example of protein interactions presented in this paper will start from the recognition and binding between a surface bound ligand and its antibody approaching from solution. Study of such a model system will help to understand the binding kinetics and mechanisms of signal transduction on cell membranes [35], which are generally initiated by the interaction between a multivalent... [Pg.65]


See other pages where Proteins recognition and binding is mentioned: [Pg.11]    [Pg.145]    [Pg.1910]    [Pg.202]    [Pg.123]    [Pg.1909]    [Pg.11]    [Pg.145]    [Pg.1910]    [Pg.202]    [Pg.123]    [Pg.1909]    [Pg.300]    [Pg.406]    [Pg.1237]    [Pg.33]    [Pg.819]    [Pg.57]    [Pg.316]    [Pg.159]    [Pg.160]    [Pg.171]    [Pg.17]    [Pg.293]    [Pg.294]    [Pg.148]    [Pg.66]    [Pg.304]    [Pg.312]    [Pg.41]    [Pg.558]    [Pg.174]    [Pg.304]    [Pg.338]    [Pg.474]    [Pg.110]    [Pg.107]    [Pg.76]    [Pg.117]    [Pg.1083]    [Pg.137]    [Pg.283]    [Pg.41]    [Pg.64]    [Pg.427]    [Pg.218]    [Pg.426]    [Pg.588]    [Pg.84]   
See also in sourсe #XX -- [ Pg.195 , Pg.196 , Pg.287 ]




SEARCH



Proteins recognition

Recognition and binding of proteins

© 2024 chempedia.info