Protein gross structure

In retrospect it is easy to see that such structural irregularity is actually required for proteins to fulfill their diverse functions. Information storage and transfer from DNA is essentially linear, and DNA molecules of very different information content can therefore have essentially the same gross structure. In contrast, proteins must recognize many thousands of different molecules in the cell by detailed three-dimensional interactions, which... 

The conformational changes which have been described so far are probably all relatively small local changes in the structure of H,K-ATPase. This has been confirmed by Mitchell et al. [101] who demonstrated by Fourier transform infrared spectroscopy that a gross change in the protein secondary structure does not occur upon a conformational change from Ei to 3. Circular dichroism measurements, however [102,103], indicated an increase in a-helical structure upon addition of ATP to H,K-ATPase in the presence of Mg and... 

In this section, we describe several statistical quantities that capture the gross structural features of the landscape. In Section II.C.l, we discuss the experimental observations of the tolerance of proteins to mutation and describe a correlation between the tolerance and the interresidue coupling. In Section II.C.2, landscape ruggedness is described in terms... 

This Chapter focuses on analyses that can be performed based solely on the primary sequence of a protein. Several rationales can be applied. Physico-chemical characteristics of individual amino acids are one basis for predictions of gross structural features. For example, particular repetitive patterns may suggest a coiled-coil structure while in general secondary structure can be predicted based on an a statistical analysis of the primary sequence. The definition of signals recognized by the cellular transport machinery allow the prediction of subcellular location. Although somewhat unsystematic such observations can provide valuable hints as to the structure and/or function of a protein. 

Two structural elements of the Raf kinase have been found to interact with the Ras protein. One structural element involved in complex formation on the c-Rafl kinase side is the Ras-binding domain, encompassing amino acids 51-131 of the CR1 domain. On the Ras protein side, the switch I region is involved in this interaction, as shown by the crystal structure of the complex between the Ras-binding domain of c-Rafl kinase and the GTP form of the Ras-like protein, RaplA protein (Nassar et ah, 1995 ). These structural studies did not reveal gross conformational changes of the two proteins upon complex formation. 

Paramyosin has not yet been extracted in the usual sense. It is obtained from certain mollusc muscles by grinding in Edsall-Weber solution, destroying the gross structure, and bringing much of the protein into solution. In such extracts the paramyosin occurs in the form of intact fibrils, which dissolve at ionic strength 0.6 (Schmitt et al, 1947). 

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