X-ray studies on crystalline complexes involving amino acids and peptides. XXI. Structure of a (1:1) complex between L-phenylalanine and D-valine


Autoria(s): Prasad, GS; Vijayan, M
Data(s)

1991

Resumo

CsHllNO2.C9HilNO2, Mr = 282.3, P1, a = 5.245 (1), b = 5.424 (1), c = 14.414 (2) A, a = 97.86 (1), fl = 93-69 (2), y = 70-48 (2) °, V= 356 A 3, Z = 1, O m = 1-32 (2), Dx = 1.32 g cm-3, h(Mo Ka) = 0-7107 A, g = 5-9 cm-1, F(000) = 158, T= 298 K, R=0.035 for 1518 observed reflections with I>2tr(I). The molecules aggregate in double layers, one ayer made up of L-phenylalanine molecules and the other of D-valine molecules. Each double layer is stabilized by interactions involving main-chain atoms of both types of molecules. The interactions include hydrogen bonds which give rise to two head-to-tail sequences. The arrangement of molecules in the complex is almost the same as that in the structure of DL-valine (and DL-leucine and DL-isoleucine) except for the change in the side chain of L molecules. The molecules in crystals containing an equal number of L and O hydrophobic amino-acid molecules thus appear to aggregate in a similar fashion, irrespective of the precise details of the side chain.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/34615/1/X-ray_Studies.pdf

Prasad, GS and Vijayan, M (1991) X-ray studies on crystalline complexes involving amino acids and peptides. XXI. Structure of a (1:1) complex between L-phenylalanine and D-valine. In: Acta Crystallographica Section C, 47 (12). pp. 2603-2606.

Publicador

International Union of Crystallography

Relação

http://scripts.iucr.org/cgi-bin/paper?S0108270191006327

http://eprints.iisc.ernet.in/34615/

Palavras-Chave #Molecular Biophysics Unit
Tipo

Journal Article

PeerReviewed