Primary macromolecular structure

Self-assembling macromolecules are particularly well suited for applications as nano- and micro-templates. Macromolecules allow control of the size and topology of the template over many decades in length scale. The simplest primary macromolecular structure which permits one to carry out these functions are diblock copolymers. The last few years have seen considerable progress in the development of methods to synthesize block polymers, some of them applicable on an industrial scale. 

The implications of the foregoing concept have profoundly influenced modern trends in polymer research. If polymers owe their differences from other compounds to the extent and arrangement of their primary valence structures, the problem of understanding them is twofold. It is necessary in the first place to provide appropriate means, both experimental and theoretical, for elucidating their macromolecular structures a[Pg.3]

The three classes of macromolecular structures can be considered at a number of increasingly complex levels, described as their primary, secondary and tertiary structures. 

Why does protein concentration exert such strong stabilizing influences on protein structure and, thereby, on enzymatic activity And why can a protein such as BSA affect the stability of an unrelated enzymatic protein like MDH To explain the effects shown in figure 6.21, another type of stabilizing influence must be introduced, one that differs from the mechanisms involving solvophobic (hydro-phobic and osmophobic) effects. The primary phenomenon involved in accounting for stabilization of macromolecular structure by other macromolecules is termed the excluded volume effect, which is one consequence of the molecu-... 

PDB The Protein Data Bank, originally compiled at Brookhaven National Laboratory and currently distributed from http //www.rcsb.org, contains X-ray diffraction and NMR-based structural data of macromolecular structures such as proteins, nucleic acids, and entire viruses. The PDB is the primary structural databank for the 3-D coordinates of macromolecules and freely accessible on-line. 

In spite of the close theoretical relationship between EPR and NMR spectroscopy, EPR has only very narrow applications. The primary reason for this is that the EPR phenomenon is spectroscopically silent unless there are unpaired electrons. Most biological macromolecules are closed shell molecules and contain no unpaired electrons. Therefore, EPR is of little real value for biological macromolecular structure characterisation. The only exception to this rule is that certain prosthetic groups in proteins may contain redox active metal centres/clusters that have transient or even permanent unpaired electrons (see Chapter 4). These metal centres/ clusters can be studied by EPR spectroscopy in order to demonstrate the presence of unpaired electrons. Thereafter, EPR data may then be used to derive the relative structural arrangements of metals within centres or clusters, and to assign putative distributions of redox states should there be any obvious redox heterogeneity. EPR is also useful to detect transient or even metastable radical formation during bio catalysis (see Chapter 8). 

Although this book is concerned with hair fibers in general, the primary focus is on human scalp hair, and this first chapter is concerned primarily with the growth, the morphology, and the macromolecular structure of this unique fiber. 

Aliphatic vinyl ketones have been reported to polymerize similarly [349,352]. Although, the introduction of the furan ring (2-furyl vinyl ketone as monomer) does not alter the mode of chain growth with radical initiation. The regularity of the macromolecular structure is, however, accompanied by a serious drawback in terms of yield. Even with very high initiator concentration, the formation of polymer stopped at about 20% conversion. This is due to the retarding effect produced by the attack of primary radical onto the furan ring rather than onto the vinylic function. 

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