| Nuclear magnetic resonance (NMR) |
1Hα and 13Cα signal shifts (ΔδHα and ΔδCα) |
53, 66, 72, 73, 83–90, 94, 99, 109, 115, 116 and 165
|
| Circular dichroism (CD) |
Maximums and minimums in the 190–250 nm CD region |
38–42, 44, 45, 48, 53, 55, 59, 60, 62, 65, 67, 70, 71, 75, 77, 83, 87, 93, 94, 97, 99, 102, 105, 109, 112, 117, 119 and 120
|
| Electron paramagnetic resonance (EPR) |
Substituted Cys or coordinated Cu2+ tracking |
96–99
|
| Fluorescence spectroscopy |
Tryptophan (Trp, 300–450 nm), tyrosine (Tyr, 250–370 nm) and phenylalanine (Phe, 250–350 nm) shifts |
39, 42, 53, 62, 64, 66, 69, 70, 71, 73, 75, 77, 87, 94, 101 and 102
|
| Raman spectroscopy |
Amide I (1630–1700 cm−1), amide III (1230–1310 cm−1) and backbone skeletal stretch (870–1150 cm−1) regions |
104–107
|
| Fourier transform infrared spectroscopy (FT-IR) |
Amide I (1700–1600 cm−1) and amide II (1600–1500 cm−1) regions |
48, 59, 60, 67, 75, 93, 106 and 109–112
|
| Small-angle X-ray scattering (SAXS) |
Form factor, Kratky plot and pair distance-distribution function (PDDF) shape |
44, 45, 52, 65, 111, 115, 116, 117 and 120
|
| Static and dynamic light scattering (SLS & DLS) |
Gyration (Rg) and hydrodynamic radius (RS) |
44, 53, 54, 55, 56, 57, 73, 75, 88, 99, 119 and 120
|
