title: Structural conformation of spidroin in solution: a synchrotron radiation circular dichroism study.
abstract: 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.
authors.affiliation: Department of Zoology, Oxford University, OX1 3PS United Kingdom. cedric.dicko@zoology.ox.ac.uk
authors.forename: Cedric
authors.initials: C
authors.lastname: Dicko
authors.forename: David
authors.initials: D
authors.lastname: Knight
authors.forename: John M
authors.initials: JM
authors.lastname: Kenney
authors.forename: Fritz
authors.initials: F
authors.lastname: Vollrath
mesh_terms: D002942:Circular Dichroism; D005349:Fibroins / Q000737:chemistry*; D011487:Protein Conformation; D011489:Protein Denaturation; D012996:Solutions; D013056:Spectrophotometry, Ultraviolet; D017356:Synchrotrons
chemical_list: D012996:Solutions; D005349:Fibroins