Application of C-Terminal 7-Azabicyclo[2.2.1]heptane to Stabilize β-Strand-like Extended Conformation of a Neighboring α-Amino Acid

2018 ◽  
Vol 83 (21) ◽  
pp. 13063-13079 ◽  
Author(s):  
Luhan Zhai ◽  
Siyuan Wang ◽  
Masayuki Nara ◽  
Koh Takeuchi ◽  
Ichio Shimada ◽  
...  
2015 ◽  
Vol 71 (4) ◽  
pp. o240-o241
Author(s):  
Sumesh Nicholas

The title peptide,N-benzyloxycarbonyl-β-glycylglycylglycine benzyl ester, C22H25N3O6, contains a non-proteinogenic amino acid residue, β-glycine, which is a homologated analogue of glycine. In the molecular structure, β-glycine adopts an extended conformation with atransconformation about its Cβ—Cαbond. The second glycine residue adopts an extended conformation while the third glycine residue adopts a helical conformation. In the crystal, three N—H...O hydrogen bonds, two involving the same carbonyl O atom as acceptor, results in an infinite two-dimensional network parallel to thebcplane.


1995 ◽  
Vol 1 (4) ◽  
pp. 157-162 ◽  
Author(s):  
André Aubry ◽  
Valerio Del Duca ◽  
Monica Pantano ◽  
Fernando Formaggio ◽  
Marco Crisma ◽  
...  

2015 ◽  
Vol 71 (4) ◽  
pp. 322-329 ◽  
Author(s):  
Krishnan Ravikumar ◽  
Balasubramanian Sridhar ◽  
Jagadeesh Babu Nanubolu ◽  
Tamilselvan Rajasekaran ◽  
Basi Venkata Subba Reddy

Four structures of oxoindolyl α-hydroxy-β-amino acid derivatives, namely, methyl 2-{3-[(tert-butoxycarbonyl)amino]-1-methyl-2-oxoindolin-3-yl}-2-methoxy-2-phenylacetate, C24H28N2O6, (I), methyl 2-{3-[(tert-butoxycarbonyl)amino]-1-methyl-2-oxoindolin-3-yl}-2-ethoxy-2-phenylacetate, C25H30N2O6, (II), methyl 2-{3-[(tert-butoxycarbonyl)amino]-1-methyl-2-oxoindolin-3-yl}-2-[(4-methoxybenzyl)oxy]-2-phenylacetate, C31H34N2O7, (III), and methyl 2-[(anthracen-9-yl)methoxy]-2-{3-[(tert-butoxycarbonyl)amino]-1-methyl-2-oxoindolin-3-yl}-2-phenylacetate, C38H36N2O6, (IV), have been determined. The diastereoselectivity of the chemical reaction involving α-diazoesters and isatin imines in the presence of benzyl alcohol is confirmed through the relative configuration of the two stereogenic centres. In esters (I) and (III), the amide group adopts ananticonformation, whereas the conformation issynin esters (II) and (IV). Nevertheless, the amide group forms intramolecular N—H...O hydrogen bonds with the ester and ether O atoms in all four structures. The ether-linked substituents are in the extended conformation in all four structures. Ester (II) is dominated by intermolecular N—H...O hydrogen-bond interactions. In contrast, the remaining three structures are sustained by C—H...O hydrogen-bond interactions.


1992 ◽  
Vol 47 (1) ◽  
pp. 90-92 ◽  
Author(s):  
Zdzisław Gałdecki ◽  
Bernard Luciak ◽  
Adam S. Redliński ◽  
Krzysztof Kaczmarek ◽  
Mirosław T. Leplawy

The compound CH3-CO-NH-C(C2H5)2-COOH was synthesized from the corresponding free amino acid. N-Acetyl-Cα,α-diethylglycine crystallizes in the monoclinic space group P21/c with a = 13.551(2)Å, b = 11.110(3)Å, c = 13.569(3)Å, β = 111.54(2)°, Z = 8 , D = 1.21 g/cm3. This structure was solved by direct methods and refined to R = 0.084. N-Acetyl-Cα,α-diethylglycine shows a fully extended conformation in its -N H-C(C2H5)2-CO- part.


Author(s):  
M.K. Lamvik ◽  
L.L. Klatt

Tropomyosin paracrystals have been used extensively as test specimens and magnification standards due to their clear periodic banding patterns. The paracrystal type discovered by Ohtsuki1 has been of particular interest as a test of unstained specimens because of alternating bands that differ by 50% in mass thickness. While producing specimens of this type, we came across a new paracrystal form. Since this new form displays aligned tropomyosin molecules without the overlaps that are characteristic of the Ohtsuki-type paracrystal, it presents a staining pattern that corresponds to the amino acid sequence of the molecule.


Author(s):  
A. J. Tousimis

The elemental composition of amino acids is similar to that of the major structural components of the epithelial cells of the small intestine and other tissues. Therefore, their subcellular localization and concentration measurements are not possible by x-ray microanalysis. Radioactive isotope labeling: I131-tyrosine, Se75-methionine and S35-methionine have been successfully employed in numerous absorption and transport studies. The latter two have been utilized both in vitro and vivo, with similar results in the hamster and human small intestine. Non-radioactive Selenomethionine, since its absorption/transport behavior is assumed to be the same as that of Se75- methionine and S75-methionine could serve as a compound tracer for this amino acid.


Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.


1979 ◽  
Vol 7 (1) ◽  
pp. 261-262
Author(s):  
E. V. ROWSELL

2001 ◽  
Vol 120 (5) ◽  
pp. A153-A153
Author(s):  
S MIYAMOTO ◽  
K KATO ◽  
Y ISHII ◽  
S ASAI ◽  
T NAGAISHI ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document