Dataset containing physical-chemical and strucutural descriptors for exclusive α-helices (only a single helical structure segment is present in the protein's whole structure) and its flanking regions.<div><br></div><div>Only alpha helices from all-α <b>proteins </b>are eligible for this dataset.<br><div><br><div>Data is organized into sections. Each section begins with the following header: <b>length, pdb_name, chain_id, flag, position, [parameter]</b>.<br></div></div><div><br></div><div><b>length</b> is the number of amino acid residues comprising the α-helix.</div><div><br></div><div><b>flag</b> indicates the amino acid residue underlying region, namely: flanking region before the α-helix (<b><</b>); α-helix (<b>=</b>); flanking region after the α-helix (<b>></b>).</div><div><br></div><div><b>[parameter]: </b>paramater's value for the given amino acid residue. All parameters are extracted from the STING Database.</div><div><br></div><div><b>Example:</b></div><div><b>Solvent-accessible surface area </b><b>for all amino acid residues forming an </b>α-helix <b>of length 6</b></div><div><b><br></b></div><div>length, pdb_name, chain_id, flag, position, Accessible_Surface_in_Isolation</div><div>6,1not,A,=,1,136.585<br></div><div><div>6,1not,A,=,2,106.068</div><div>6,1not,A,=,3,11.322</div><div>6,1not,A,=,4,49.517</div><div>6,1not,A,=,5,227.67</div><div>6,1not,A,=,6,110.9</div></div><div><b><br></b></div></div
