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Domains function evolution

Fig. 5 LEEM images showing domain pattern evolution as a function of Pb coverage at 673 K. The images correspond to Pb coverages of (a) 0.33, (b) 0.39, and (c) 0.48 ML. The evolution from droplets to stripes to inverted droplets is evident. Figure from Ref. [68]. Fig. 5 LEEM images showing domain pattern evolution as a function of Pb coverage at 673 K. The images correspond to Pb coverages of (a) 0.33, (b) 0.39, and (c) 0.48 ML. The evolution from droplets to stripes to inverted droplets is evident. Figure from Ref. [68].
Ivies Z, Izsvak Z, Minter A, Hackett PB (1996) Identification of functional domains and evolution of Tcl-like transposable elements. Proc Natl Acad Sci USA 93 5008-5013. [Pg.538]

In order to make as much data on the structure and its determination available in the databases, approaches for automated data harvesting are being developed. Structure classification schemes, as implemented for example in the SCOP, CATH, andFSSP databases, elucidate the relationship between protein folds and function and shed light on the evolution of protein domains. [Pg.262]

In the most basic implementation of 2D acquisition, a series of free induction decays are recorded as a function of the first evolution period (l time domain), starting at the beginning of the second evolution period (h time domain), instead of at the top of the isotropic echoes. The phase of the signal is... [Pg.152]

This evolution can be studied either in time domain, by following the recurrences of the correlation function ... [Pg.129]

The use of sequence information to frame structural, functional, and evolutionary hypotheses represents a major challenge for the postgeno-mic era. Central to an understanding of the evolution of sequence families is the concept of the domain a structurally conserved, genetically mobile unit. When viewed at the three-dimensional level of protein structure, a domain is a compact arrangement of secondary structures connected by linker polypeptides. It usually folds independently and possesses a relatively hydrophobic core (Janin and Chothia, 1985). The importance of domains is that they cannot be divided into smaller units— they represent a fundamental building block that can be used to understand the evolution of proteins. [Pg.185]

To facilitate cross referencing between the names of domain families used in this article and structural, functional, and evolution information available from the literature, the domain names used by the WWW-based resource SMART (http //smart.embl-heidelberg) are shown in bold and in a proportional font. [Pg.210]


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See also in sourсe #XX -- [ Pg.93 , Pg.94 ]




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