Aminoacid sequence

At the N-terminal end of the f loop, near the membrane lipid interface, there is an autoinhibitory domain, rich in both basic and hydrophobic residues and consisting of a 20-aminoacid sequence (219-238). This aminoacid sequence, named exchange inhibitory peptide (XDP), is involved in NCX activity regulation. 

Na+-dependent inactivation. There is a sequence of 20-aminoacids (219-23 8), located in the intracellular f loop near the membrane lipid interface, that seems to be involved in the Na+-dependent inactivation. This autoinhibitory 20-aminoacid sequence might interact with another portion of the f loop (562-679) producing NCX inhibition. In accordance with this view, the synthetic peptide provided with the same sequence of XIP region blocks NCX activity. 

P. diminuta 7 [320,368] N-terminal aminoacid sequence PIR Swiss-Prot Q51697 (a) and Q51698 ((3). S. Fetzner... 

Fig. 19. Lipopeptides with the aminoacid sequence of the Ras C-terminus and the natural or artificial lipid-modifications can be coupled with C-terminally truncated Ras via a maleimi-docaproyl linker. This electrophile reacts with free thiol groups (here, a C-terminal cysteine at the Ras moiety)...

Figure 2. Phylogenetic tree of cloned human aminergic GPCRs aminoacid sequences.

N-terminai aminoacid sequence of human fibroblast interferon MET SER - TYR -A5N LEU... 

Aminoacid sequences of hemeperoxidases Catalase - Bovine liver - (Bos taurus)... 

Complex aminoacid sequences structure Thiophilic like ligands Hydrophobic charge transfer effect... 

Actually antibodies are either directed against a continuous aminoacid sequence, the continuous epitopes, or a domain which is located on various sites in the aminoacid chain, discontinuous epitopes, or conformational epitopes. Continuous epitopes have served as affinity ligands for antibody... 

B8. Bonde, M., Garnero, P., Fledelius, C., Qvist, P., Delmas, P. D., and Christiansen, C., Measurement of bone degradation products in serum using antibodies reactive with an isomerized form of an 8 aminoacid sequence of the C-telopeptide of type collagen I. J. Bone Miner. Res. 12,1028—1034 (1997). 

Y. Sugimoto, K. Yatsunami, M. Tsujimoto, H. G. Khorana, and A. Ichikawa. The aminoacid sequence of a glutamic acid-rich protein from bovine retina as deduced from the cDNA sequence. Proc Nad Acad. Set, USA, 88, 3116-3119, 1991. 

Trackman, P. C., Pratt, A. M., Wolanski, A., Tang, S.-S., Offer, G. D., Troxler, R. F., and Kagan, H. M., 1990, Cloning of rat lysyl oxidase cDNA complete codons and predicted aminoacid sequences. Biochemistry 29 4863ii4870. 

Tyrosine PPs are classified in four families, depending on their biological function and aminoacid sequence tyrosine-specific phosphatases (TSPs), vaccinia virus HI (VHl)-like phosphatases, cdc25 phosphatases... 

Postiethwaite, A.E. and Seyer, J.M. (1991). Fibroblast chemotaxis induction by human recombinant interleukin-4 identification by synthetic peptide analysis of two chemotactic domains residing in aminoacid sequences 70-78 and 89-122. J. CUn. Invest. 87, 2147-2152. 

Fractional factorial designs in principal properties have also been used to design aminoacid sequences in peptides in studies on quantitative structure activity relations. [10]... 

Fig. 11. The structure of IgM. (a) The monomeric unit. This schematic representation relies greatly on comparison of the aminoacid sequence of IgM (ju chain) and IgG (y chain) and extrapolation from known features of IgG structure. The Fab arms arc as for IgG, the paired CM2 domains replace the hinge, the CM3 domains are suggested to resemble the Cy2 domains in IgG, being unpaired with interposed carbohydrate, and the CM4 domains to resemble the paired C 3 domains of IgG. A disulphide bridge connects the heavy chains between the CM2 and CM3 domains. An additional feature is a tailpiece of 18 residues at the carboxy-termini of the heavy chains which may fold back across the CM4 domains. The molecular weight of the monomer is —19(11)0(1.

The two proteins are quite similar in structure and have similar aminoacid sequences, so it seems almost certain that they are derived from a common ancestral protein that was also able to bind oxygen. Presumably it resembled myoglobin more than hemoglobin, as myoglobin is somewhat simpler in structure than hemoglobin, and it was certainly needed for binding oxygen in the... 

The surface activity of proteins (as well as many of their other functions) depends on the so-called tertiary structure of protein molecules, which is determined by the spatial arrangement of their polypeptide chains. This tertiary molecular structure depends in turn on the primary protein structure - the aminoacid sequence, which is determined by the genetic code of a cell. The surface of a protein globule is mosaic-like it contains both polar... 

Due to the complex enzyme structure the active site components are generally far apart in the linear aminoacid sequence. 

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