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Proteins and assemblies

I Sugars (sucrose, glucose, mannose) Surface tension increase Inert Good stabilizers of globular proteins and assembled organelles... [Pg.711]

Glycerol, polyols (sorbitol, mannitol) Solvophobicity Affinity for polar regions Stabilizers of globular proteins and assembled organelles, decreasing for proteins of high polarity... [Pg.711]

As seen in the genetic map, the genes after gene 1.1, transcribed by the T7 RNA polymerase, code for proteins that are involved in T7 DNA synthesis, the formation of virus coat proteins, and assembly. Three classes of T7 proteins are formed class I, made 4-8 minutes after infection, which use the cell RNA polymerase class II, made 6-15 minutes after infection, which are made from T7 RNA polymerase and are involved in DNA metabolism class III, made from 6 minutes to lysis, which are transcribed by T7 RNA polymerase and which code for phage assembly and coat protein. This sort of sequential pattern, commonly seen in many large double-stranded DNA phages, results in an efficient channeling of host resources, first toward DNA metabolism and replication, then on to formation of virus particles and release of virus by cell lysis. [Pg.142]

Figure 5.19 Simplified genetic map of T4. Late genes with morphogenetic functions (coat proteins and assembly), and genes with functions in DNA replication are identified. Note that although the genetic map is represented as a circle, the DNA itself is actually linear. Figure 5.19 Simplified genetic map of T4. Late genes with morphogenetic functions (coat proteins and assembly), and genes with functions in DNA replication are identified. Note that although the genetic map is represented as a circle, the DNA itself is actually linear.
H27. Hoffman, J. S., and Benditt, E. P., Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. J. Biol. Chem. 257, 10518-10522 (1982). [Pg.279]

Flament S, Delacourte A, Hemon B, Defossez A (1989) Characterization of two pathological tau protein, variants in Alzheimer brain cortices. J Neurol Sci 92 133-141 Friedhoff P, von Bergen M, Mandelkow EM, Mandelkow E (2000) Structure of tau protein and assembly into paired helical filaments. Biochim Biophys Acta 1502 122-132... [Pg.662]

Vondriska, T.M., Pass, J.M. and Ping, P. (2004) Scaffold proteins and assembly of multiprotein signaling complexes. J. Mol. Cell Cardiol. 37, 391-397. [Pg.182]

Production of coat proteins and assembly of complete particles... [Pg.66]

CDDB http //www.cdyn.org/ Conformational dynamics of proteins and assemblies... [Pg.25]

Only properly folded proteins and assembled subunits are transported from the rough ER to the Golgi complex in vesicles. [Pg.680]

Plenary 4. George J Thomas Jr et at, e-mail address thomasgj ,cctr.mnkc.edu (RS). Protein folding and assembly into superstructures. (Slow) time resolved RS probing of virus construction via protein assembly into an icosahedral (capsid) shell. [Pg.1217]

In biological systems molecular assemblies connected by non-covalent interactions are as common as biopolymers. Examples arc protein and DNA helices, enzyme-substrate and multienzyme complexes, bilayer lipid membranes (BLMs), and aggregates of biopolymers forming various aqueous gels, e.g, the eye lens. About 50% of the organic substances in humans are accounted for by the membrane structures of cells, which constitute the medium for the vast majority of biochemical reactions. Evidently organic synthesis should also develop tools to mimic the Structure and propertiesof biopolymer, biomembrane, and gel structures in aqueous media. [Pg.350]

Fig. 5. Protein folding. The unfolded polypeptide chain coUapses and assembles to form simple stmctural motifs such as -sheets and a-hehces by nucleation-condensation mechanisms involving the formation of hydrogen bonds and van der Waal s interactions. Small proteins (eg, chymotrypsin inhibitor 2) attain their final (tertiary) stmcture in this way. Larger proteins and multiple protein assembhes aggregate by recognition and docking of multiple domains (eg, -barrels, a-helix bundles), often displaying positive cooperativity. Many noncovalent interactions, including hydrogen bonding, van der Waal s and electrostatic interactions, and the hydrophobic effect are exploited to create the final, compact protein assembly. Further stmctural... Fig. 5. Protein folding. The unfolded polypeptide chain coUapses and assembles to form simple stmctural motifs such as -sheets and a-hehces by nucleation-condensation mechanisms involving the formation of hydrogen bonds and van der Waal s interactions. Small proteins (eg, chymotrypsin inhibitor 2) attain their final (tertiary) stmcture in this way. Larger proteins and multiple protein assembhes aggregate by recognition and docking of multiple domains (eg, -barrels, a-helix bundles), often displaying positive cooperativity. Many noncovalent interactions, including hydrogen bonding, van der Waal s and electrostatic interactions, and the hydrophobic effect are exploited to create the final, compact protein assembly. Further stmctural...
With remarkable accuracy, Democritus in the fifth century B.C. set the stage for modem chemistry. His atomic theory of matter, which he formulated without experimental verification, still stands, more or less intact, and encapsulates the profound truth that nature s stunning wealth boils down to atoms and molecules. As science uncovers the mysteries of the world around us, we stand ever more in awe of nature s ingenious molecular designs and biological systems nucleic acids, saccharides, proteins, and secondary metabolites are four classes of wondrous molecules that nature synthesizes with remarkable ease, and uses with admirable precision in the assembly and function of living systems. [Pg.1]


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See also in sourсe #XX -- [ Pg.321 ]




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