Short Sequential and Medium-Range 1H-1H Distance in Polypeptide Secondary Structures
|
| Distance |
α-helix |
310 helix |
β |
βp |
turn Ia |
turn IIa |
| dα,N |
3.5 |
3.4 |
2.2 |
2.2 |
3.4
3.2 |
2.2
3.2 |
| dα,N (i, i+2) |
4.4 |
3.8 |
- |
- |
3.6 |
3.3 |
| dα,N (i, i+3) |
3.4 |
3.3 |
- |
- |
3.1 - 4.2 |
3.8 - 4.7 |
| dα,N (i, i+4) |
4.2 |
- |
- |
- |
- |
- |
| dNN |
2.8 |
2.6 |
4.3 |
4.2 |
2.6
2.4 |
4.5
2.4 |
| dNN (i, i+2) |
4.2 |
4.1 |
- |
- |
3.8 |
4.3 |
| dβN |
2.5 - 4.1 |
2.9 - 4.4 |
3.2 - 4.5 |
3.7 - 4.7 |
2.9 - 4.4
3.6 - 4.6 |
3.6 - 4.6
3.6 - 4.6 |
| dβN (i, i+3)b |
5.3 - 5.7 |
5.0 - 5.7 |
- |
- |
- |
- |
| a For the turns, the first two numbers applies to the distance between residues 2 and 3, the
second to that between residues 3 and 4. The range indicated for dN (i, i+3) corresponds
to the distances adopted if ψ1 varied between -180 and 180o.
b The ranges given correspond to the distances adopted by a β-methine proton if χ1 is varied
between -180 and 180o. |
Reference
K. Wüthrich, M. Billeter and W. Braun, Polypeptide secondary structure determination by nuclear magnetic
resonance
observation of short proton-proton distances,J. Mol. Biol. 180 (1984), pp. 715-740.
|
