Role of proline … proline interactions in the packing of collagenlike poly(tripeptide) triple helices

✍ Scribed by George Némethy; Harold A. Scheraga

• Publisher: Wiley (John Wiley & Sons)
• Year: 1984
• Tongue: English
• Weight: 986 KB
• Volume: 23
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360231207

✦ Synopsis

Conformational energy computations were carried out on the packing of two identical collagenlike poly(tripeptide) triple helices in order to determine the energetics of favorable packing arrangements as a function of composition and chain length. The triple helices considered were [CH,CO-(Gly-Pro-Pro),,NHCH3], and [CH,CO-(Gly-Pro-Ala).; NHCH313, with n, = 3,4, and 5. The packing arrangements were characterized in terms of their intermolecular energies and orientation angles no of the axes of the two triple helices. For short triple helices (n, = 3 or 41, many low-energy orientations, with a wide range of values of no, can occur. When the triple helices are longer (n, = 5). the only low-energy packing arrangements of two poly(G1y-Pro-Pro) triple helices are those with a nearly parallel orientation of the two helix axes, with no = -10". This result .accounts * To whom reprint requests should be addressed