Random coiled Order

How does the polymer chain sneak out from the entangled random coil state and how does it order into a crystalline state ... 

This thermodynamic behaviour is consistent with stress-induced crystallisation of the rubber molecules on extension. Such crystallisation would account for the decrease in entropy, as the disorder of the randomly coiled molecules gave way to well-ordered crystalline regions within the specimen. X-Ray diffraction has confirmed that crystallisation does indeed take place, and that the crystallites formed have one axis in the direction of elongation of the rubber. Stressed natural rubbers do not crystallise completely, but instead consist of these crystallites embedded in a matrix of essentially amorphous rubber. Typical dimensions of crystallites in stressed rubber are of the order of 10 to 100 nm, and since the molecules of such materials are typically some 2000 nm in length, they must pass through several alternate crystalline and amorphous regions. 

There are two broad kinds of polyion conformation the random coil and the ordered helix. In a helix there are regularly repeated structures along the coil there are none in the case of a random coil. In this book we are concerned with the latter where there are often several conformations with approximately equal free energies and, thus, conformational changes occur readily. 

To obtain statistically significant comparisons of ordered and disordered sequences, much larger datasets were needed. To this end, disordered regions of proteins or wholly disordered proteins were identified by literature searches to find examples with structural characterizations that employed one or more of the following methods (1) X-ray crystallography, where absence of coordinates indicates a region of disorder (2) nuclear magnetic resonance (NMR), where several different features of the NMR spectra have been used to identify disorder and (3) circular dichroism (CD) spectroscopy, where whole-protein disorder is identified by a random coil-type CD spectrum. 

To further our understanding of the behavior of unfolded proteins, it is necessary to employ experimental techniques able to discriminate between the dynamic true random coil state and more static types of disorder, including situations in which some ordered secondary structure may also be present. One such technique is a novel chiroptical... 

Tanford (1968) reviewed early studies of protein denaturation and concluded that high concentrations of Gdm-HCl and, in some cases, urea are capable of unfolding proteins that lack disulfide cross-links to random coils. This conclusion was largely based on intrinsic viscosity data, but optical rotation and optical rotatory dispersion (ORD) [reviewed by Urnes and Doty (1961) ] were also cited as providing supporting evidence. By these same lines of evidence, heat- and acid-unfolded proteins were held to be less completely unfolded, with some residual secondary and tertiary structure. As noted in Section II, a polypeptide chain can behave hydrodynamically as random coil and yet possess local order. Similarly, the optical rotation and ORD criteria used for a random coil by Tanford and others are not capable of excluding local order in largely unfolded polypeptides and proteins. The ability to measure the ORD, and especially the CD spectra, of unfolded polypeptides and proteins in the far UV provides much more incisive information about the conformation of proteins, folded and unfolded. The CD spectra of many unfolded proteins have been reported, but there have been few systematic studies. 

In contrast to the reconciliation of short-range structure with net random coil-like behavior, the presence of long-range order in even the most highly denatured states is perhaps more problematic (Shortle and... 

The crystallization process of flexible long-chain molecules is rarely if ever complete. The transition from the entangled liquid-like state where individual chains adopt the random coil conformation, to the crystalline or ordered state, is mainly driven by kinetic rather than thermodynamic factors. During the course of this transition the molecules are unable to fully disentangle, and in the final state liquid-like regions coexist with well-ordered crystalline ones. The fact that solid- (crystalline) and liquid-like (amorphous) regions coexist at temperatures below equilibrium is a violation of Gibb s phase rule. Consequently, a metastable polycrystalline, partially ordered system is the one that actually develops. Semicrystalline polymers are crystalline systems well removed from equilibrium. 

P.-G. de Gennes later also considered the multisegment attraction regime. He suggested the so-called p-cluster model [11] in order to explain certain anomalies in behavior observed in many polymer species such as polyethyle-neoxide (PEO) see also [12]. The scenario of coil-globule transition with dominating multisegment interaction first considered by I.M. Lifshitz has been recently studied in [13]. The authors used a computer simulation of chains in a cubic spatial lattice to show that collapse of the polymer can be due to crystallization within the random coil. 

I have reported so far only on one non-specific adsorption, that of random coils. Thus, ordered monolayers of polymers were rare and randomly packed first layers the rule. There are of course many other types of macromolecules and their adsorption, and an... 

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