Structural conformation of spidroin in solution: A synchrotron radiation circular dichroism study

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Structural conformation of spidroin in solution : A synchrotron radiation circular dichroism study. / Dicko, Cedric; Knight, David; Kenney, John M.; Vollrath, Fritz.

In: Biomacromolecules, Vol. 5, No. 3, 01.05.2004, p. 758-767.

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Dicko, Cedric ; Knight, David ; Kenney, John M. ; Vollrath, Fritz. / Structural conformation of spidroin in solution : A synchrotron radiation circular dichroism study. In: Biomacromolecules. 2004 ; Vol. 5, No. 3. pp. 758-767.

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TY - JOUR

T1 - Structural conformation of spidroin in solution

T2 - Biomacromolecules

AU - Dicko, Cedric

AU - Knight, David

AU - Kenney, John M.

AU - Vollrath, Fritz

PY - 2004/5/1

Y1 - 2004/5/1

N2 - Spider silk is made and spun in a complex process that tightly controls the conversion from soluble protein to insoluble fiber. The mechanical properties of the silk fiber are modulated to suit the needs of the spider by various factors in the animal's spinning process. In the major ampullate (MA) gland, the silk proteins are secreted and stored in the lumen of the ampulla. A particular structural fold and functional activity is determined by the spidroins' amino acid sequences as well as the gland's environment. The transition from this liquid stage to the solid fiber is thought to involve the conversion of a predominantly unordered structure to a structure rich in beta-sheet as well as the extraction of water. Circular dichroism provides a quick and versatile method for examining the secondary structure of silk solutions and studying the effects of various conditions. Here we present the relatively novel technique of synchrotron radiation based circular dichroism as a tool for investigating biomolecular structures. Specifically we analyze, in a series of example studies on structural transitions induced in liquid silk, the type of information accessible from this technique and any artifacts that might arise in studying self-assembling systems.

AB - Spider silk is made and spun in a complex process that tightly controls the conversion from soluble protein to insoluble fiber. The mechanical properties of the silk fiber are modulated to suit the needs of the spider by various factors in the animal's spinning process. In the major ampullate (MA) gland, the silk proteins are secreted and stored in the lumen of the ampulla. A particular structural fold and functional activity is determined by the spidroins' amino acid sequences as well as the gland's environment. The transition from this liquid stage to the solid fiber is thought to involve the conversion of a predominantly unordered structure to a structure rich in beta-sheet as well as the extraction of water. Circular dichroism provides a quick and versatile method for examining the secondary structure of silk solutions and studying the effects of various conditions. Here we present the relatively novel technique of synchrotron radiation based circular dichroism as a tool for investigating biomolecular structures. Specifically we analyze, in a series of example studies on structural transitions induced in liquid silk, the type of information accessible from this technique and any artifacts that might arise in studying self-assembling systems.

UR - http://www.scopus.com/inward/record.url?scp=2542535248&partnerID=8YFLogxK

U2 - 10.1021/bm034373e

DO - 10.1021/bm034373e

M3 - Article

VL - 5

SP - 758

EP - 767

JO - Biomacromolecules

JF - Biomacromolecules

SN - 1526-4602

IS - 3

ER -