Molecular evolution, intracellular organization, and the quinary structure of proteins.
書誌事項
- 公開日
- 1982-05
- DOI
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- 10.1073/pnas.79.10.3236
- 公開者
- Proceedings of the National Academy of Sciences
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説明
<jats:p>High-resolution two-dimensional polyacrylamide gel electrophoresis shows that at least half of 370 denatured polypeptides from hamster cells and human cells are indistinguishable in terms of isoelectric points and molecular weights. Molecular evolution may have been more conservative for this set of proteins than sequence studies on soluble proteins have implied. This may be a consequence of complexities of intracellular organization and the numerous macromolecular interactions in which most polypeptides participate. It is suggested that the term "quinary structure" be used to refer to macromolecular interactions that are transient in vivo. Such interactions will not be evident from the composition of purified proteins, but they may constitute an important source of constraints on changes in primary structure.</jats:p>
収録刊行物
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- Proceedings of the National Academy of Sciences
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Proceedings of the National Academy of Sciences 79 (10), 3236-3240, 1982-05
Proceedings of the National Academy of Sciences