Abstract
The relationship between amino acid sequence, three-dimensional structure
and
biological function of proteins is one of the most intensely pursued areas
of
molecular biology and biochemistry. In this context, the three-dimensional
structure has a pivotal role, its knowledge being essential to understand
the
physical, chemical and biological properties of a protein (Branden &
Tooze, 1991;
Creighton, 1993). Until 1984 structural information at atomic resolution
could
only be determined by X-ray diffraction techniques with protein single
crystals
(Drenth, 1994). The introduction of nuclear magnetic resonance (NMR)
spectroscopy (Abragam, 1961) as a technique for protein structure determination
(Wüthrich, 1986) has made it possible to obtain structures with comparable
accuracy also in a solution environment that is much closer to the natural
situation
in a living being than the single crystals required for protein crystallography.
Publisher
Cambridge University Press (CUP)
Cited by
147 articles.
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