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. Author manuscript; available in PMC: 2014 Apr 16.
Published in final edited form as: Langmuir. 2013 Apr 2;29(15):4839–4846. doi: 10.1021/la4000846

Table 1.

Physico-chemical characteristics of selected carbon binding peptides

Name Sequencea Mr (Da) pI Hydropathyb
Car9 graphic file with name nihms464024t1.jpg 1346.6 11.1 −1.900
Car14 graphic file with name nihms464024t2.jpg 1200.3 4.3 +0.267
Car15 graphic file with name nihms464024t3.jpg 1431.8 8.8 +0.525
Car16 graphic file with name nihms464024t4.jpg 1409.6 9.6 −1.000
a

Amino acids are color-coded as follows: hydrophobic, gray; acidic, red; basic, cyan; hydroxyl side chain, green; aromatic (yellow). Invariant tripeptides flanking the dodecamers are italicized.

b

Average hydropathy score are based on the Kyte and Doolittle scale.53 Positive scores denote hydrophobic sequences while negative scores denote hydrophilic sequences. The higher (respectively, lower) the score, the more hydrophobic (respectively, hydrophilic) the sequence is.