AbstractNew conformational data for members of the series Boc‐(D‐Val)m‐(L‐Val‐D‐Val)(n‐m)/2‐OMe (m = 0 or 1; n = total number of residues) are presented and used together with earlier results to formulate general conclusions regarding types and relative stabilities of ß‐helices formed by D,L‐alternating valine peptides. The helices, single‐ or double‐stranded, are of the tightest geometry, the single‐stranded helices having only 4,4 residues per turn(ß4,4 ‐helices) and the double‐stranded ones only about 5,6 residues per turn (↑↓ß5,6‐and ↑↑ß5,6‐helices). The double‐stranded helices are of the type with the highest possible number of interstrand H‐bonds [2(n‐1)] and the antiparallel ones are always strongly preferred. In chloroform solution right‐and left‐handed ß4,4‐helices and left‐handed ↑↓ß5,6 and ↑↑szlig;5,6‐helices are formed by the oligovalines studied with different preferences depending on the peptide chain length and on the parity of the number (odd or even) of residues. The reasons for these preferences are discussed.