Table 1.
Protein | α‐helix | β‐sheet | turn | other | NRMSD | CATH | |
---|---|---|---|---|---|---|---|
HBN | S | 73 ± 3 | 2 ± 1 | 9 ± 0 | 15 ± 3 | 0.020 | |
F | 70 ± 5 | 2 ± 1 | 9 ± 1 | 17 ± 6 | 0.060 | ||
PDB | 77 | 0 | 23 | 1.10.490.10 | |||
MBN | S | 73 ± 2 | 1 ± 1 | 10 ± 0 | 17 ± 3 | 0.011 | |
F | 65 ± 7 | 4 ± 4 | 11 ± 1 | 22 ± 6 | 0.038 | ||
PDB | 74 | 0 | 26 | 1.10.490.10 | |||
CYC | S | 38 ± 1 | 14 ± 4 | 13 ± 1 | 35 ± 2 | 0.033 | |
F | 37 ± 2 | 15 ± 3 | 12 ± 1 | 35 ± 2 | 0.042 | ||
PDB | 37 | 0 | 63 | 1.10.760.10 | |||
CHM | S | 20 ± 0 | 21 ± 1 | 15 ± 0 | 43 ± 1 | 0.051 | |
F | 33 ± 4 | 11 ± 1 | 17 ± 1 | 40 ± 4 | 0.048 | ||
PDB | 12 | 32 | 56 | 2.40.10.10 | |||
ELA | S | 9 ± 2 | 32 ± 3 | 15 ± 1 | 44 ± 0 | 0.072 | |
F | 15 ± 1 | 27 ± 1 | 15 ± 0 | 43 ± 1 | 0.068 | ||
PDB | 10 | 30 | 60 | 2.40.10.10 | |||
CON | S | 9 ± 3 | 40 ± 2 | 11 ± 1 | 38 ± 1 | 0.057 | |
F | 8 ± 3 | 41 ± 2 | 12 ± 1 | 38 ± 1 | 0.108 | ||
PDB | 4 | 46 | 50 | 2.60.120.200 | |||
RNS | S | 23 ± 1 | 29 ± 1 | 12 ± 1 | 35 ± 1 | 0.040 | |
F | 18 ± 1 | 31 ± 1 | 12 ± 1 | 38 ± 1 | 0.056 | 3.10.130.10 | |
PDB | 21 | 33 | 46 | ||||
CAH | S | 11 ± 3 | 35 ± 2 | 12 ± 0 | 40 ± 1 | 0.085 | |
F | 12 ± 3 | 35 ± 2 | 13 ± 1 | 41 ± 2 | 0.115 | ||
PDB | 16 | 29 | 55 | 3.10.200.10 | |||
APO | S | 23 ± 1 | 23 ± 1 | 11 ± 2 | 44 ± 2 | 0.019 | |
F | 45 ± 8 | 11 ± 7 | 13 ± 1 | 33 ± 6 | 0.125 | ||
PDB | 21 | 24 | 55 | 4.10.410.10 |
Secondary structures of the proteins in solution (S), in films (F), and calculated from PDB files using the DSSP algorithm. Their CATH classification is also listed. The values determined from the solutions and films are the average calculations derived from 3 different algorithms, with the ± values indicating the S.D. between the methods, and the NRMSD is a goodness‐of‐fit parameter. The protein names are abbreviated as: HBN, hemoglobin; MBN, myoglobin; CYC, cytochrome C; CHM, alpha‐chymotrypsin; ELA, elastase; CON, concanavalin A; RNS, ribonuclease A; CAH, carbonic anhydrase II; and APO, bovine trypsin inhibitor (aprotinin).