“…The crystal structures of amino acids with hydrophobic side chains invariably incorporate molecular bilayers, each with a hydrogen-bonded core and two surfaces shaped by the amino acid side chains. A series of unique solid-state phase transitions, involving sliding along the hydrophobic interfaces between adjacent bilayers, have been observed for dlmethionine (Met; Mathieson, 1952;Taniguchi et al, 1980;Alagar et al, 2005;Gö rbitz et al, 2014; Gö rbitz, 2014), dl-2-aminobutyric acid (Abu; Gö rbitz et al, 2012; Nakata et al, 1980;Voogd & Derissen, 1980;Akimoto & Iitaka, 1972;Ichikawa & Iitaka, 1968), dl-norvaline (Nva; Gö rbitz, 2011) and dl-norleucine (Nle; Coles et al, 2009;Harding et al, 1995;Dalhus & Gö rbitz, 1996b;Smets et al, 2015;van den Ende & Cuppen, 2014) as well as for the four quasiracemates l-Nva:d-Nle, l-Nva:d-Met, l-Nle:d-Met (Gö rbitz & Karen, 2015) and l-Abu:d-Met (Gö rbitz et al, 2016). Little is known by comparison about the corresponding enantiomeric amino acids.…”