Amino acid sequences, availability

What can be done by predictive methods if the sequence search fails to reveal any homology with a protein of known tertiary structure Is it possible to model a tertiary structure from the amino acid sequence alone There are no methods available today to do this and obtain a model detailed enough to be of any use, for example, in drug design and protein engineering. This is, however, a very active area of research and quite promising results are being obtained in some cases it is possible to predict correctly the type of protein, a, p, or a/p, and even to derive approximations to the correct fold. 

From this brief review of marine vertebrate venoms, it is obvious that very few biochemical investigations have been done. The technology to study marine vertebrate venom components is available. There are simply not enough scientists interested enough to enter the field. The first task is to isolate the toxic principles and identify the amino acid sequences. Pharmacological investigation should be done on the purified toxic principle and not on the crude venom, which is a mixture of many proteins and nonproteins. 

It Is hoped that current work being carried out on the amino acid sequence of human PTH (1-4) will be successful, so that synthetic preparations of Important regions of the hormone can become commercially available. This would partially... 

An mRNA of 8.8 kb was detected in rat uterus and stomach [32], which is different from the mRNAs of PMCAl-3 and may represent a distinct member of the PMCA series. Its amino acid sequence is not yet available. 

A complete amino acid sequence for cytochrome c from N. crassa is available (81). In the case of U. sphaerogena, only an amino acid composition has been determined. U. sphaerogena forms a relatively large amount... 

Upon its generation, sequence information is normally submitted to various databases. The major databases in which protein primary sequence data are available are listed in Table 2.4. Also included in this table are the major nucleic acid sequence databases, as amino acid sequence information can potentially be derived from these. 

The molecular replacement method assumes similarity of the unknown structure to a known one. This is the most rapid method but requires the availability of a homologous protein s structure. The method relies on the observation that proteins which are similar in their amino acid sequence (homologous) will have very similar folding of their polypeptide chains. This method also relies on the use of Patterson functions. As the number of protein structure determinations increases rapidly, the molecular replacement method becomes extremely useful for determining protein phase angles. 

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