Intricate three-dimensional

Or the hardener can deprotonate a hydroxyl group from the interior of a chain, cross-linking one chain with another. The final polymer is an intricate three-dimensional network that is strong and resistant to chemical attack. 

It is possible to make very intricate, three-dimensional carvings in ihino horn. This work was common on old ihino horn items such as libation and diinkii cups, and dagger handles C ig. 6.3). 

Sequence comparison is a powerful tool for extending our knowledge of protein function and kinship. However, biomolecules generally function as intricate three-dimensional structures rather than as linear polymers. Mutations occur at the level of sequence, but the effects of the mutations are at the level of function, and function is directly related to tertiary structure. Consequently, to gain a deeper understanding of evolutionary relationships between proteins, we must examine three-dimensional structures, especially in conjunction with sequence information. The techniques of structural determination are presented in Chapter 4. 

Protein chains fold into intricate three-dimensional structures. 

The specificity of an enzyme is due to the precise interaction of the substrate with the enzyme. This precision is a result of the intricate three-dimensional structure of the enzyme protein. 

Higher temperatures may disrupt the intricate three dimensional stracture of the enzyme, thereby reducing or totally destroying its catalytic activity. 

Intricate three-dimensional shapes are crucial to protein functioning. These shapes come about by cross-linking between various biochemical functional groups (mostly amino acids) on the long-chain protein molecule (King et al., 2002). It is the cross-linking among these elanents that provides the motivation and the stability of protein structure. 

Figure 95). The two remaining pyridyl groups participate in hydrogen bonding with included water molecules. An intricate three-dimensional framework results (Figure 96). 

It is known that a large part of the tertiary structure of some proteins consists of packed helical segments. As the temperature increases, these helices unfold and attain a random coil conformation. The transition from the helical to the random coil is similar to the denaturation process. Therefore it is believed that the study of the helix-coil transition is an essential step in the understanding of the denaturation process. It is known, however, that protein denaturation is a far more complex process. It involves the breakdown of an intricate three-dimensional tertiary structure, only part of which is the helix-coil transition. Some proteins do not even contain substantial content of helical structure. Therefore, the study of this particular transition will not give us the answer to the far more complex denaturation process. In the rest of this section we shall focus on the theory of the helix-coil transition only. We shall return to the folding-unfolding process of proteins in Chapter 8. 

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