. Author manuscript; available in PMC: 2011 Jan 11.

Published in final edited form as: Biomacromolecules. 2010 Jan 11;11(1):192–200. doi: 10.1021/bm9010672

Table 2.

Percent β-sheet and helical structure in N. clavipes major (Ma) and minor (Mi) ampullate spider silk predicted from the consensus primary amino acid sequence (AA %) and extracted from the curve fits to NMR data shown in figure 3 and 4 (NMR %)

	Major Silk				Minor Silk

	β-sheet		helical		β-sheet		helical
	AA (%)	NMR (%)	AA (%)	NMR (%)	AA (%)	NMR (%)	AA (%)	NMR (%)
Ala	86	82 ± 4	14	18 ± 4	75^‡ - 83^†	77 ± 2	17^† - 25^‡	23 ± 2
Gly	26	28 ± 5	74	72 ± 5	44^‡- 52^†	53 ± 2	48^†- 56^‡	47 ± 2
Ser	19	21 ± 2	81	79 ± 2	41^†- 48^‡	52 ± 1	52^‡- 59^†	48 ± 1

The amount of MiSp1 and MiSp2 is not known for Nephila clavipes minor ampullate silk (Mi). The percent amino acid in pure MiSp1^† and MiSp2^‡ represent the range of possible concentrations for minor ampullate silk.