Back Cover: Monoprotected l -Amino Acid (l -MPAA), Accelerated Bromination, Chlorination, and Iodination of C(sp2 )−H Bonds by Iridium(III) Catalysis (Chem. Eur. J. 29/2017)

2017 ◽  
Vol 23 (29) ◽  
pp. 7153-7153
Author(s):  
Subban Kathiravan ◽  
Ian A. Nicholls
Keyword(s):  
Amino Acid ◽  
Back Cover

scholarly journals Back Cover: Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues (Chem. Eur. J. 16/2015)

2015 ◽  
Vol 21 (16) ◽  
pp. 6304-6304
Author(s):  
Gábor Olajos ◽  
Anasztázia Hetényi ◽  
Edit Wéber ◽  
Lukács J. Németh ◽  
Zsolt Szakonyi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Back Cover ◽  
Induced Folding

scholarly journals Back Cover: Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations (Chem. Eur. J. 48/2016)

2016 ◽  
Vol 22 (48) ◽  
pp. 17488-17488
Author(s):  
Debora Scuderi ◽  
Enrico Bodo ◽  
Barbara Chiavarino ◽  
Simonetta Fornarini ◽  
Maria Elisa Crestoni
Keyword(s):  
Amino Acid ◽  
Acid Oxidation ◽  
Irmpd Spectroscopy ◽  
Amino Acid Oxidation ◽  
Back Cover

scholarly journals Back Cover: Corrole and Porphyrin Amino Acid Conjugates: Synthesis and Physicochemical Properties (Chem. Eur. J. 32/2016)

2016 ◽  
Vol 22 (32) ◽  
pp. 11472-11472
Author(s):  
Kostas Karikis ◽  
Evangelos Georgilis ◽  
Georgios Charalambidis ◽  
Athanasia Petrou ◽  
Olena Vakuliuk ◽  
...  
Keyword(s):  
Amino Acid ◽  
Physicochemical Properties ◽  
Amino Acid Conjugates ◽  
Back Cover

The staining pattern of the tropomyosin sequence is displayed in a new paracrystal

1986 ◽  
Vol 44 ◽  
pp. 150-151
Author(s):  
M.K. Lamvik ◽  
L.L. Klatt
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Staining Pattern ◽  
Banding Patterns ◽  
Mass Thickness ◽  
New Form

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.

Electron probe x-ray microanalysis and electron microscopy of amino acid absorption and transport by the small intestine: inhibition by chemical poisons and correlation to the elemental composition of the epithelial cells

1986 ◽  
Vol 44 ◽  
pp. 134-135
Author(s):  
A. J. Tousimis
Keyword(s):  
Small Intestine ◽  
Amino Acid ◽  
Epithelial Cells ◽  
Elemental Composition ◽  
Isotope Labeling ◽  
Structural Components ◽  
X Ray ◽  
Human Small Intestine ◽  
Transport Studies

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.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

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.

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