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. Author manuscript; available in PMC: 2014 Feb 14.
Published in final edited form as: J Phys Chem B. 2013 Feb 4;117(6):1790–1809. doi: 10.1021/jp3097378

Table 1.

Folding of Hairpin Peptides at 280 K. a

Substitutions pH % Foldedb
none 6.5 91.0
Ala8/ε-N-acetyl-Lys 8 6.5 93.6
Ala8Asn 6.5 92.4
Ala8Asp 6.5 88.0
2.5 89.4
Ala8Lys 6.5 91.5
Ala8Cha c 6.5 98.5
Ala8Gln 6.5 92.0
Ala8Glu 6.5 89.1
Ala8Ser 6.5 94.5
Ala8Cys 8 6.0 84.5
10.5 48.9
Ala8Orn c 6.5 92.1
Ala8Tyr 6.0 91.7
10.67 90.7
Ala8His 7.85 97.7
2.5 94.9
Phe10Tyr 6.5 90.4
10.7 99.0
Phe10His 7.85 66.6
2.5 65.9
Phe10Leu 6.5 59.1
Trp1N-Ac-Phe / Phe10Trp 6.5 41.1
a

The peptides are Ac-WVTIpGKAIFTG-NH2 with the indicated substitutions for residues in bold font. Except where indicated (last row), all the peptides had Trp at position 1.

b

Chemical-shift deviations of the following atoms were used to calculate the % folding: Val2 NH, Ile3 Hα, Ile4 NH, X8 Hα, Ile9 NH, and when X = Phe or Tyr, X10 Hβ3 and X10 Hδ.

c

Abbreviations: Cha = cyclohexylalanine, Orn = ornithine.