Proteins and function

Imataka, H., Gradi, A., and Sonenberg, N. (1998). A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBOJ. 17, 7480-7489. 

In the conventional methods of proteomics, 2-DE and MS use such approaches working backward from the fractionated proteins to their corresponding DNA sequences. Unfortunately, these approaches represent a significant bias toward the abundant proteins, and functionally important proteins of low abundance are often not detected by this way. 

Figure 5.33 Mechanism of the receptor-mediated induction of CYP1A1 by a polycyclic hydrocarbon such as TCDD. The inducer-receptor (AhR) complex enters the nucleus, binds with ARNT, and the complex binds to the CYP1A1 gene in the DNA. This induces the production of CYP1A1 mRNA, which leads to the production of CYP1A1 protein and functional enzyme. Abbreviations AIP, AhR interacting protein AhR, aryl hydrocarbon receptor HSP, heat shock protein 90 ARNT, AhR nuclear translocator E.R., endoplasmic reticulum.

Most cytochromes have only one heme group per polypeptide chain,112 but the 115-residue cytochrome c3 from the sulfate-reducing bacterium Desulfovibrio binds four hemes (Fig. 16-8C).104,113 115 Each one seems to have a different redox potential in the -0.20 to -0.38 V range.114 Another c-type cytochrome, also from Desulfovibrio, contains six hemes in a much larger 66-kDa protein and functions as a nitrite reductase.116... 

In CHO cells, stably expressing human A3 AR, a prolonged treatment with the NECA agonist (20 h), induces uncoupling of the receptor from Gi-protein and functional desensitisation associated with a reduction in the number of the high affinity binding sites, in accordance with the data about the rat A3 AR. 

Carraro Alleoni, A.C. 2006. Albumen protein and functional properties of gelation and foaming. SciAgric (Piracicaba, Braz.) 63(3) 291—298. 

Cholesterol and membrane proteins, including structural ones such as glycophorin and myelin basic protein and functional ones such as -ATPase, bacteriorhodopsin, and cytochrome c, are important components of biological membranes. Cholesterol-lipid and a number of protein-lipid interactions have therefore been extensively investigated by vibrational spectroscopy. Interactions of hormones and toxins with phospholipid bilayers were also investigated. 

In the field of biology, the effects of hydration on equilibrium protein structure and dynamics are fundamental to the relationship between structure and biological function [21-27]. In particular, the assessment of perturbation of liquid water structure and dynamics by hydrophilic and hydrophobic molecular surfaces is fundamental to the quantitative understanding of the stability and enzymatic activity of globular proteins and functions of membranes. Examples of structures that impose spatial restriction on water molecules include polymer gels, micelles, vesicles, and microemulsions. In the last three cases since the hydrophobic effect is the primary cause for the self-organization of these structures, obviously the configuration of water molecules near the hydrophilic-hydrophobic interfaces is of considerable relevance. 

Maes M, Schaipe S, Meltzer HY, Bosnians E, Suy E, Calabrese J, Cosyns P (1993) Reladonsliips between interleukin-6 activity, acute phase proteins, and function of tlie hypotlialainic-pituitai y-adrenal axis in severe depression. Psycliiati y Res 49 11—27. 

Many physiological functions have been linked to specific subtypes of ar, o -, and (3-adrenergic receptors in various animal species. Because of the obvious reason of limited access, particularly regarding healthy tissue, similar progress for human adrenergic receptors has been slower and in many cases limited to the characterization of expression of RNA for the receptor subtypes. A more extensive characterization of protein and function for all the human adrenergic receptor subtypes is needed to identify specific targets for possible therapeutic intervention. 

Pond AL, Nerbonne JM. 2001. ERG proteins and functional cardiac Iki channels... 

The effect of lincomycin resistance mutations in Escherichia Coli on the alteration of ribosomal proteins and functions was analyzed by Hummel et al (74). The results show that lincomycin did not seem to alter any ribosomal function. 

LBM includes skeletal muscle, somatic protein, and functional proteins such as circulating proteins and the visceral proteins. Biochemically, LBM can be assessed by measuring the serum visceral proteins, albumin (ALB), transferrin (TFN), and prealbumin (thyroxine-binding prealbumin or transthyretin). Other serum proteins, such as retinol-binding protein, flbronectin (an opsonic protein), and somatomedin-C (insulin-like growth factor-1), that have a very short half-life (less than 12 to 24 hours), have been suggested as... 

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