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Structures and functionalization nature

Figure 8. Structures and functionalization nature of poly(styrene) derivatives reacted with TiClj. Figure 8. Structures and functionalization nature of poly(styrene) derivatives reacted with TiClj.
Rabenstein, D. L. (2002). Heparin and heparan sulfate Structure and function. Natural Product Reports, 19(3), 312-331. [Pg.538]

Geisow M (1977) Serum albumin structure and function. Nature 270 476-477... [Pg.97]

Weber, PC., Salemme, ER. Structural and functional diversity in 4-a-helical proteins. Nature 287 82-84, 1980. [Pg.46]

Alin, A. H., and Knnkel, L. M., 1993. The. structural and functional diver-.sity of dy.strophin. Nature Genetics 3 283-291. [Pg.563]

Hu J, Spiegel AM (2003) Naturally occurring mutations of the extracellular Ca2+-sensing receptor implications for its structure and function. Trends Endocrinol Metab 14 282-288... [Pg.305]

Section 4.5). Of these, mesocosms have stimulated the greatest interest. In these, replicated and controlled tests can be carried out to establish the effects of chemicals upon the structure and function of the (artihcial) communities they contain. The major problem is relating effects produced in mesocosms to events in the real world (see Crossland 1994). Nevertheless, it can be argued that mesocosms do incorporate certain relationships (e.g., predator/prey) and processes (e.g., carbon cycle) that are found in the outside world, and they test the effects of chemicals on these. Once again, the judicious use of biomarker assays during the course of mesocosm studies may help to relate effects of chemicals measured by them with similar effects in the natural environment. [Pg.323]

Proteins derive their powerful and diverse capacity for molecular recognition and catalysis from their ability to fold into defined secondary and tertiary structures and display specific functional groups at precise locations in space. Functional protein domains are typically 50-200 residues in length and utilize a specific sequence of side chains to encode folded structures that have a compact hydrophobic core and a hydrophilic surface. Mimicry of protein structure and function by non-natural ohgomers such as peptoids wiU not only require the synthesis of >50mers with a variety of side chains, but wiU also require these non-natural sequences to adopt, in water, tertiary structures that are rich in secondary structure. [Pg.18]

In striated muscle, there are two other proteins that are minor in terms of their mass but important in terms of their function. Tropomyosin is a fibrous molecule that consists of two chains, alpha and beta, that attach to F-actin in the groove between its filaments (Figure 49-3). Tropomyosin is present in all muscular and muscle-fike structures. The troponin complex is unique to striated muscle and consists of three polypeptides. Troponin T (TpT) binds to tropomyosin as well as to the other two troponin components. Troponin I (Tpl) inhibits the F-actin-myosin interaction and also binds to the other components of troponin. Troponin C (TpC) is a calcium-binding polypeptide that is structurally and functionally analogous to calmodulin, an important calcium-binding protein widely distributed in nature. Four molecules of calcium ion are bound per molecule of troponin C or calmodulin, and both molecules have a molecular mass of 17 kDa. [Pg.562]

From the atomic to the macroscopic level chirality is a characteristic feature of biological systems and plays an important role in the interplay of structure and function. Originating from small chiral precursors complex macromolecules such as proteins or DNA have developed during evolution. On a supramolecular level chirality is expressed in molecular organization, e.g. in the secondary and tertiary structure of proteins, in membranes, cells or tissues. On a macroscopic level, it appears in the chirality of our hands or in the asymmetric arrangement of our organs, or in the helicity of snail shells. Nature usually displays a preference for one sense of chirality over the other. This leads to specific interactions called chiral recognition. [Pg.135]

When a virus multiplies, the genome becomes released from the coat. This process occurs during the infection process. The present chapter is divided into three parts. The first part deals with basic concepts of virus structure and function. The second part deals with the nature and manner of multiplication of the bacterial viruses (bacteriophages). In this part we introduce the basic molecular biology of virus multiplication. The third part deals with important groups of animal viruses, with emphasis on molecular aspects of animal virus multiplication. [Pg.108]

The reason is basically the same story we learned above about why the kinds of functional biology cannot be identified with those of molecular biology. Because the same functional role can be realized by a diversity of structures, and because natural selection encourages this diversity, the full macromolecular explanation for (PS) or for (G) will have to advert to a range of physical systems that realize independent assortment in many different ways. These different ways will be an unmanageable disjunction of alternatives so great that we will not be able to recognize what they... [Pg.131]


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Natural structures

Structure and Functionality

Structure and function

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