Hypotheses that correlate the sequence, structure, and mechanical properties of spider silk proteins

Int J Biol Macromol. Mar-Apr 1999;24(2-3):271-5. doi: 10.1016/s0141-8130(98)00089-0.

Abstract

Several types of silks and silk protein coding genes have been characterized from orb-web weaving spiders. When the protein sequences of major ampullate, minor ampullate, and flagelliform silks from Nephila clavipes are compared, they can be summarized as sets of shared amino acid motifs. Four of these motifs and their likely secondary structures are described. Each structural element, termed a module, is then associated with its impact on the mechanical properties of a silk fiber. In particular, correlations are drawn between an alanine-rich 'crystalline module' and tensile strength and between a proline-containing 'elasticity module' and extensibility.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Insect Proteins / chemistry*
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Silk
  • Spiders / chemistry*

Substances

  • Insect Proteins
  • Silk