A SIMPLIFIED STRATEGY FOR SEQUENCE ANALYSIS OF LARGE PROTEINS
A SIMPLIFIED STRATEGY FOR SEQUENCE ANALYSIS OF LARGE PROTEINS
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DOI:
10.1038/193241a0
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发表时间:
1962-01-01
期刊:
影响因子:
64.8
通讯作者:
ECK, RV
中科院分区:
文献类型:
--
作者:
ECK, RV
STRATEGY which appears theoretically much more efficient than the usual stepwise procedures for determining amino-acid sequences has been tested in a “paper experiment” with a “protein” of 400 links. This strategy suggested itself during work in preparation for the protein cryptogram**. In compiling published data on amino-acid sequences, no attempt was usually made to evaluate the 1 elative reliability of each datum. Instead, the cryptogram calculations were planned in such a way that occasional errors in the data could be tolerated. However, an exception had to be made in the case of the structuro of lysozyme.Two laboratories had reported voluminous results, each accounting for almost all the empirical formula, which showed quite extensive disagreement. Jollès and his school had used various enzymes and special treatments of the original protein. The intact protein (132 links) was considered to be too large for direct analysis, so enzymes were used to reduce it to medium-sized chains, which were then separated, purified, and analysed by acid hydrolysis and other methods. About half the linkages wero finally identified, and most of the remainder represented by composition analyses of large products of enzyme digestion".