The high-performance mechanical properties of certain spider silks can be r
adically altered by the addition of water. For example, unconstrained silk
fibers from the major ampullate gland of the golden orb-weaving spider, Nep
hila clavipes, contract to about half of their original length when immerse
d in water. In this paper we use solid-state C-13 and H-2 NMR to study N. c
lavipes silk fibers, so as to address the molecular origins of supercontrac
tion in the wet silk. Using C-13 NMR, we study backbone dynamics and demons
trate that, when in contact with water, a substantial fraction of the glyci
ne, glutamine, tyrosine, serine, and leucine residues in the protein backbo
ne show dramatic increases in the rate of large-amplitude reorientation. 2H
NMR of silk samples that incorporate leucine deuterated at one terminal me
thyl group provides a probe for dynamics at specific side chains along the
fiber. Only a subset of these leucine residues is strongly affected by wate
r. We suggest that the highly conserved YGGLGS(N)QGAGR blocks found in the
silk protein play a major role in the supercontraction process. Amino acid
sequences are proposed to produce artificial spider silk with similar mecha
nical properties, but without the undesired phenomenon of supercontraction.
A possible use of the "supercontracting sequence" is also suggested.