Results 161 to 170 of about 73,063 (216)

The achiral tetrapeptideZ-Aib-Aib-Aib-Gly-OtBu

Acta Crystallographica Section C Structural Chemistry, 2014
The title achiral peptideN-benzyloxycarbonyl-α-aminoisobutyryl-α-aminoisobutyryl-α-aminoisobutyrylglycinetert-butyl ester orZ-Aib-Aib-Aib-Gly-OtBu (Aib is α-aminoisobutyric acid,Zis benzyloxycarbonyl, Gly is glycine and OtBu indicates thetert-butyl ester), C26H40N4O7, is partly hydrated (0.075H2O) and has two different conformations which together ...
Renate, Gessmann   +2 more
openaire   +2 more sources

Conformational Analysis of the Cyclic Pentadepsipeptide Cyclo(Tro‐Aib‐Aib‐Aib‐Aib) in the Solid State and in Solution

Helvetica Chimica Acta, 2001
The cyclic 16-membered pentadepsipeptide cyclo(Tro-Aib-Aib-Aib-Aib) (1) was crystallized from MeOH/AcOEt/CH2Cl2, and its structure was established by X-ray crystallography (Fig. 1). There are two symmetry-independent molecules with different conformations in the asymmetric unit. Two intramolecular H-bonds stabilize two beta-turns in each molecule.
Koch, Kristian N   +4 more
openaire   +1 more source

Crystal structure of Z-Aib-Aib-Aib-Ala-Ala-Aib-OtBu, a hexapeptide fragment of trichotoxin

Biochemical and Biophysical Research Communications, 1986
The crystal structure of Z-Aib-Aib-Aib-Ala-Ala-Aib-OtBu, an end-protected hexapeptide with a sequence corresponding to residues 7-12 of several trichotoxin A-50 sequence analogues has been determined by X-ray crystallography. The hexapeptide adopts a right-handed 3(10)-helical conformation consisting of four consecutive beta-turns of type III.
M, Kokkinidis   +2 more
openaire   +2 more sources

The first non‐helical Aib‐containing hexapeptide: The crystal structure of Z‐Gly‐Aib‐Gly‐Aib‐Gly‐Aib‐OtBu

Journal of Peptide Science, 2021
The synthetic peptide Z‐Gly‐Aib‐Gly‐Aib‐Gly‐Aib‐OtBu was crystallized from a mixture of ethyl acetate and n‐hexane. The crystals belong to the centrosymmetric space group Pbca. There are three molecules in the asymmetric unit. The three molecules differ mainly in the Z‐group conformation.
Renate Gessmann   +2 more
openaire   +2 more sources

Helix packing of leucine‐rich peptides: A parallel leucine ladder in the structure of Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe

Proteins: Structure, Function, and Bioinformatics, 1992
AbstractThe packing of peptide helices in crystals of the leucine‐rich decapeptide Boc‐Aib‐Leu‐Aib‐Aib‐Leu‐Leu‐Leu‐Aib‐Leu‐Aib‐OMe provides an example of ladder‐like leucylleucyl interactions between neighboring molecules. The peptide molecule forms a helix with five 5→1 hydrogen bonds and two 4→1 hydrogen bonds near the C terminus.
Karle, Isabella L   +3 more
openaire   +2 more sources

AIBS

Bulletin of the Entomological Society of America, 1963
E. A. Steinhaus, R. F. Smith
openaire   +1 more source

AIBS News: AIBS Task Force for the '90s

BioScience, 1990
Paul R. Ehrlich   +2 more
openaire   +1 more source

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