منابع مشابه
Redetermination of poly[μ-chlorido-heptachlorido-μ3-l-proline-μ2-l-proline-tetramercury(II)]
The asymmetric unit of the title compound, [Hg(4)Cl(8)(C(5)H(9)NO(2))(2)](n), consists of four HgCl(2) units and two L-proline ligands in the zwitterionic form. In each HgCl(2) unit, the Hg(II) ion is strongly bonded to two Cl atoms, and the Hg(II) ions in two of the HgCl(2) units are chelated by O atoms of two l-proline ligands, with one strong and one weak Hg-O bond. In the crystal structure,...
متن کاملCrystal structure of catena-poly[[cadmium(II)-di-μ2-bromido-μ2-l-proline-κ2 O:O′] monohydrate]
In the title coordination polymer, {[CdBr2(C5H9NO2)]·H2O} n , the Cd(II) ion is coordinated by four bromido ligands and two carboxyl-ate oxygen atoms of two symmetry-related proline ligands, which exist in a zwitterionic form, in a distorted octa-hedral geometry. There is an intra-molecular N-H⋯O hydrogen bond between the amino group and the carboxyl-ate fragment. Each coordinating ligand bridg...
متن کاملPolymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline).
Poly(L-prolyl-glycyl-L-proline) closely resembles collagen in its X-ray diffraction pattern, which indicates that it has a triple-helical structure with the same helical parameters as the protein. A detailed conformational analysis has been made of the polytripeptide. A computer was used systematically to generate structures having the observed helical parameters, as well as standard bond lengt...
متن کاملConformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure.
Late embryogenesis abundant (LEA) proteins are members of a large group of hydrophilic, glycine-rich proteins found in plants, algae, fungi, and bacteria known collectively as hydrophilins that are preferentially expressed in response to dehydration or hyperosmotic stress. Group 2 LEA (dehydrins or responsive to abscisic acid) proteins are postulated to stabilize macromolecules against damage b...
متن کاملRaman optical activity of tetra-alanine in the poly(l-proline) II type peptide conformation.
The poly(l-proline) II (PPII) helix is considered to be a major conformation in disordered polypeptides and unfolded proteins in aqueous solution. The PPII conformation can be identified by using Raman optical activity (ROA), which measures the different intensities of right- and left-circularly polarized Raman scattered light from chiral molecules and provides information on stereochemistry as...
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ژورنال
عنوان ژورنال: Acta Crystallographica
سال: 1959
ISSN: 0365-110X
DOI: 10.1107/s0365110x59002535