The fact that an object, for example, a protein, possesses a three-dimensional structure seems an obvious concept. However, when the object is flexible, the concept is less obvious. Growing experimental data over several decades show that proteins are not rigid objects, but they may sample more or less wide ranges of different conformations. To stress this concept, we propose to call the range of sampled conformations the “fourth dimension” of the protein structure. Nuclear magnetic resonance is a precious technique to define this fourth dimension. Examples of conformational heterogeneity taken from the realm of metalloproteins and their functional implications are discussed.
"Four-dimensional" protein structures: Examples from metalloproteins / M. Fragai; C. Luchinat; G. Parigi. - In: ACCOUNTS OF CHEMICAL RESEARCH. - ISSN 0001-4842. - STAMPA. - 39:(2006), pp. 909-917. [10.1021/ar050103s]
"Four-dimensional" protein structures: Examples from metalloproteins
FRAGAI, MARCO;LUCHINAT, CLAUDIO;PARIGI, GIACOMO
2006
Abstract
The fact that an object, for example, a protein, possesses a three-dimensional structure seems an obvious concept. However, when the object is flexible, the concept is less obvious. Growing experimental data over several decades show that proteins are not rigid objects, but they may sample more or less wide ranges of different conformations. To stress this concept, we propose to call the range of sampled conformations the “fourth dimension” of the protein structure. Nuclear magnetic resonance is a precious technique to define this fourth dimension. Examples of conformational heterogeneity taken from the realm of metalloproteins and their functional implications are discussed.File | Dimensione | Formato | |
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