Possible formation of the left-handed α-helix of poly-L-serine.

Abstract:

:A conformational study of poly-L-serine has shown that it can exist in the left-handed α-helical form. A study of a pair of peptide units with the serine sidegroup attached to the α carbon atom linking the two units showed that OH ⃛O hydrogen bonds between the OH group of the side chain and a carbonyl oxygen of the first peptide group in the backbone can occur in two regions of ϕ, namely, ϕ = 15°-30° for χ1 = 300° and for ϕ = 225°-230° for ϕ = 60°. The latter is close to a possible left-handed helix of poly-L-serine, stabilized by NH ⃛O hydrogen bonds. From a study of contact criteria, the best conformation for this helix is found to be ϕ = 227°, Ψ = 238°, χ1 = 65° which has n = 3.65, h = 1.51 A. The NH ⃛O hydrogen bond has a length of 2.90 A. (6°) and the OH ⃛O hydrogen bond is of length 2.60 A. (0°). There are no other bad short contacts in the structure. The cylindrical coordinates of the atoms, as well as a perspective view of the structure arc given in this paper.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Sarathy KP,Ramachandran GN

doi

10.1002/bip.1968.360060403

subject

Has Abstract

pub_date

1968-04-01 00:00:00

pages

461-467

issue

4

eissn

0006-3525

issn

1097-0282

journal_volume

6

pub_type

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