Protein servings

G-Protein Coupling. The heterotrimeric guanosine triphosphate (GTP) binding proteins, known as G-proteins, are a principal family of proteins serving to couple membrane receptors of the G-protein family to ionic and biochemical processes. This topic is reviewed in References 63—67. 

Proteins can be broadly classified into fibrous and globular. Many fibrous proteins serve a stmctural role (11). CC-Keratin has been described. Fibroin, the primary protein in silk, has -sheets packed one on top of another. CoUagen, found in connective tissue, has a triple-hehcal stmcture. Other fibrous proteins have a motile function. Skeletal muscle fibers are made up of thick filaments consisting of the protein myosin, and thin filaments consisting of actin, troponin, and tropomyosin. Muscle contraction is achieved when these filaments sHde past each other. Microtubules and flagellin are proteins responsible for the motion of ciUa and bacterial dageUa. 

Richmond and collaborators (Figure 12.30). The octamer (Figure 12.29) has surface landmarks that guide the course of the DNA around the octamer 146 bp of B-DNA in a flat, left-handed superhelical conformation make 1.65 turns around the histone core (Figure 12.30), which itself is a protein superhelix consisting of a spiral array of the four histone dimers. Histone 1, a three-domain protein, serves to seal the ends of the DNA turns to the nucleosome core and to organize the additional 40 to 60 bp of DNA that link consecutive nucleo-... 

Protein (Section 26.4) A large peptide containing 50 or more amino acid residues. Proteins serve both as structural materials and as enzymes that control an organism s chemistry. 

In mitochondria (Fig. lb), the electron acceptor protein is also a flavoprotein termed NADPH-adrenodoxin reductase (MW 50 kDa) because it was discovered in the adrenal cortex and because it donates its electrons not directly to the P450 but to the smaller redox protein adrenodoxin (MW 12.5 kDa). The two iron-sulphur clusters of this protein serve as electron shuttle between the flavoprotein and the mitochondrial P450. 

Ananthan, J., Goldberg, A.L., Voellmy, R. (1986). Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. ScietKe 232,522-524. 

Important products derived from amino acids include heme, purines, pyrimidines, hormones, neurotransmitters, and biologically active peptides. In addition, many proteins contain amino acids that have been modified for a specific function such as binding calcium or as intermediates that serve to stabilize proteins—generally structural proteins—by subsequent covalent cross-hnk-ing. The amino acid residues in those proteins serve as precursors for these modified residues. Small peptides or peptide-like molecules not synthesized on ribosomes fulfill specific functions in cells. Histamine plays a central role in many allergic reactions. Neurotransmitters derived from amino acids include y-aminobutyrate, 5-hydroxytryptamine (serotonin), dopamine, norepinephrine, and epinephrine. Many drugs used to treat neurologic and psychiatric conditions affect the metabolism of these neurotransmitters. 

The G-protein serves as a timekeeper and binds GTP, and with GTP bound, it can couple the receptor and activate the adenylate cyclase. However, the G-protein slowly hydrolyzes the bound GTP to GDP and Pj. When this happens, the whole complex falls apart and the adenylate kinase is inactivated. 

The advantage of such co-purification protocols is that the fully processed protein serving as the bait can allow interactions in a native environment and cellular location to allow isolation of multicomponent complexes. One limitation with this approach is the necessity for an antibody with specific immunoreactivity and immunoprecipitative capability for the bait protein. This drawback can be addressed by expression of the protein with an epitope tag. Excellent antibodies to a variety of epitope tags are available and can be utilized for immunoaffinity purification. Tags such as 6-histidine and GST allow purification using affinity characteristics to nickel and GSH beads, respectively. 

Together, all the inferences from both computational modeling and simulation (which can reveal novel aspects of the receptor mechanisms, based on the dynamic properties of the proteins) serve as mechanistic working hypotheses for new and more focused experiments. This mode of closely considered interactions and synergy between computational developments and experimental probing of the receptor systems has become a sustained characteristic of current studies of structure-function... 

Figure 8 (Plate 7). Structure of the Escherichia coli FhuA protein serving as receptor for ferrichrome and the antibiotic albomycin. (a) side view (b) side aspect with partly removed barrel to allow the view on the cork domain (c) top view. A single lipo-polysaccharide molecule is tightly associated with the transmembrane region of FhuA (reproduced by permission of W. Welte and A. Brosig)...

The acute-phase response is characterised by the enhanced (two- to threefold) synthesis of a number of proteins, such as antiproteinases, complement components, fibrinogen and ceruloplasmin, which are normally synthesised at fairly low rates. The rate of synthesis of some proteins is enhanced 100-1000-fold - for example, C-reactive protein, a-macroglobulin and acid-1-glycoprotein. Thus, serum levels of these proteins serve as indicators of disease. 

F-box proteins serve as the substrate-targeting subunit of the SCF ubiquitin E3 ligase [5]. They are structurally diverse but they all contain a relatively conserved signature motif of about 45-50 amino acids [5]. This motif, the F-box, was initially... 

P-Glycoprotein (P-gp), a member of the adenosine triphosphate (ATP)-binding cassette family of membrane transporters, is encoded by the human multidrug-resistance (MDRl, ABCBl) gene (15). This integral membrane protein serves as an... 

Before we take leave of primary structures for proteins, there is one last, important realization. Proteins serving the same function in different species may have different primary structures. For example, the primary structures of bovine, ovine, and human insulins are not quite the same. They are closely related but not identical. Different species have discovered different protein solutions for the same biological problem. 

One might well imagine that the primary structures for proteins serving the same function in different species would most resemble each other for species that are closely related in an evolutionary sense. Such proteins are termed homologs. This turns out to be the case. Cytochrome c is a protein very widely distributed throughout nature. The primary structure for the cytochrome c of humans is very similar to that from pigs but not quite so similar to that from frogs and even more distantly related to that from insects and, at the extreme, that of wheat. 

Proteins serving the same function in different species may have different primary structures. The extent of the differences is a measure of their relatedness on the evolutionary tree of life. 

Iron-sulfur proteins serve predominantly as electron carriers (28,29). The best understood examples are those proteins with IFe, 2Fe, and 4Fe centers. The environment of the mononuclear iron center, rubredoxin, is shown in structure C (17). It consists of a distorted tetrahedral array of sulfur atoms from cysteine residues at nearly equal distances from the iron atom. Crystal structures are available for 2Fe-2S ferredoxins from Spindina plantensis (19) and Aphanothece sacrum (20). A representation of the geometry of this site is given in structure D. The 2Fe-2S core is anchored to the polypeptide by ligation to 4 cysteine sulfur atoms, yielding distorted tetrahedral geometry for both iron atoms. Crystal... 

Lipoproteins are classified into five groups. In order of decreasing size and increasing density, these are chylomicrons, VLDLs (very-low-density lipoproteins), IDLs (inter-mediate-density lipoproteins), LDLs (low-density lipoproteins), and HDLs (high-density lipoproteins). The proportions of apoproteins range from 1 % in chylomicrons to over 50% in HDLs. These proteins serve less for solubility purposes, but rather function as recognition molecules for the membrane receptors and enzymes that are involved in lipid exchange. 

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