ATP-lipids - Protein anchor and energy source in two dimensions

DOI: 10.1021/ja953937m

Source and publish data:

Journal of the American Chemical Society p. 5532 - 5543 (1996)

Update date:2022-08-03

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Authors:

Schmitt, Lutz

Tampé, Robert

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Article abstract of DOI:10.1021/ja953937m

The ubiquitous function of ATP as energy equivalent in nature has resulted in a common folding pattern of ATP-binding proteins. Their binding pocket tolerates modifications of the adenine ring to some extend, whereas those of the triphosphate group strong

Full text of DOI:10.1021/ja953937m

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