Distance distributions in proteins: a six-parameter representation.
We present a statistical analysis of protein structures based on interatomic C alpha distances. The overall distance distributions reflect in detail the contents of sequence-specific substructures maintained by local interactions (such as alpha-helixes) and longer range interactions (such as disulfide bridges and beta-sheets). We also show that a volume scaling of the distances makes distance distributions for protein chains of different length superimposable. Distance distributions were also calculated specifically for amino acids separated by a given number of residues. Specific features in these distributions are visible for sequence separations of up to 20 amino acid residues. A simple representation, which preserves most of the information in the distance distributions, was obtained using six parameters only. The parameters give rise to canonical distance intervals and when predicting coarse-grained distance constraints by methods such as data-driven artificial neural networks, these should preferably be selected from these intervals. We discuss the use of the six parameters for determining or reconstructing 3-D protein structures.
Reese
M G
MG
Department of Physics, Technical University of Denmark, Lyngby, Denmark.
Lund
O
O
Bohr
J
J
Bohr
H
H
Hansen
J E
JE
Brunak
S
S
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D016208:Databases, Factual; D015394:Molecular Structure; D011487:Protein Conformation; D015202:Protein Engineering; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics
D000596:Amino Acids; D011506:Proteins