Folding characteristics

To explain the folding characteristics of Tetrahymena ribozyme, a simple generalization of counterion condensation model was proposed [108, 109], In this two state model, equilibrium is considered between condensed and free counterions [108]. The chemical potential for each phase is approximately calculated as follows. If the volume fraction occupied by the counterions is denoted by < ), then the chemical potential of the free counterions is [108]... 

The general purpose film grade is biaxially oriented , a property that gives it stability at temperatures up to 130 °C. They also offer a biaxially oriented film for high temperature applications (150 °C). According to NatureWorks, these resins offer excellent optical properties, good machinability and excellent twist and dead fold characteristics. These polymers are offered in common pellet form, which should allow for rapid adoption with conventional extruders. 

Independent folding regions within a protein. The group/pattern of secondary structures forming a Domain s tertiary structure is called a Fold. (Characteristic bond type hydrophobic others hydrogen, ion-pair, van der Waals.)... 

Figure 5 Folding characteristics of tailed proteins. The effects of the length of the attached flexible tail on the protein s thermostability (a) and the protein s radius of gyration in the unfolded state (the tails were attached to an SH3 domain at residue 36). The stability and radius of gyration changes are...

As described in the introduction, RNAz calculates various folding characteristics to classify the alignment. These are displayed in the header section of the RNAz output. 

As mentioned earlier, foil can be found as a single layer material and applied as an overwrap using the dead fold characteristics of soft foil. Thin foil can be partly strengthened by embossing, but due to its extensibility it tends to demand an additional support ply. 

Exhibits dead-fold characteristics—stays relatively flat when folded. 

Fold—overwrapping without sealing, fold over, fold down, grocer s fold, roll wrap, bread wrap, etc. Note dead fold characteristic of soft foil (see BS 1133) and overwrapping, plus seal—i.e. heat, adhesive, etc. 

The image robustness of a solid ink can be substantially improved by incorporating a small amount of a copol m er from ethylene and vinyl acetate (36). Such inks exhibit improved scratch and fold characteristics. 

Lowik et demonstrated that the secondary structure of certain peptide sequences conjugated to single Ci8 alkyl chains at both the N- and C-termini could be induced upon incorporation into a liposome membrane. A sequence derived from the circumsporozoite (CS) protein of the malaria parasite Plasmodium falciparum was chosen, as within the natural protein the Asn-Pro-Asn-Ala repeat is known to adopt a j6-tum. Both the unmodified peptide in solution and the analogous peptide with only one alkyl chain showed random coil folding characteristics. However, when the double alkylated peptide was inserted into l,2-dimyristoyl-OT-glycero-3-phosphoethanol-amine (DSPC) liposomes the peptide folded into a P-hairpin. This simple approach is a convenient way for stabilizing a variety of peptides into their preferred secondary structure and might be employed in the presentation of multiple (hairpin) epitopes. 

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