Vibrational spectra and crystal structure of the di-amino acid peptide cyclo(L -Met-L -Met): comparison of experimental data and DFT calculations

2009 ◽  
Vol 41 (2) ◽  
pp. 148-159 ◽  
Author(s):  
Andrew P. Mendham ◽  
Brian S. Potter ◽  
Rex A. Palmer ◽  
Trevor J. Dines ◽  
John C. Mitchell ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Experimental Data ◽  
Amino Acid ◽  
Dft Calculations ◽  
Vibrational Spectra ◽  
Amino Acid Peptide

Vibrational spectroscopy and DFT calculations of the di-amino acid peptide l-aspartyl-l-glutamic acid in the zwitterionic state

2009 ◽  
Vol 11 (30) ◽  
pp. 6389 ◽  
Author(s):  
Nighat Kausar ◽  
Trevor J. Dines ◽  
Babur Z. Chowdhry ◽  
Bruce D. Alexander
Keyword(s):  
Amino Acid ◽  
Dft Calculations ◽  
Glutamic Acid ◽  
Vibrational Spectroscopy ◽  
Amino Acid Peptide

Refined Crystal Structure and Absolute Configuration of the Di-amino Acid Peptide Cyclo(l-Aspartyl-l-Aspartyl): Comparison with the DFT Calculated Structure

2010 ◽  
Vol 40 (7) ◽  
pp. 608-615 ◽  
Author(s):  
Rex A. Palmer ◽  
Brian S. Potter ◽  
Andrew P. Mendham ◽  
Trevor J. Dines ◽  
Babur Z. Chowdhry
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Absolute Configuration ◽  
Amino Acid Peptide

On the Reaction of Hexachlorocyclotriphosphazene with Heptamethyldisilazane. Crystal Structure of P3N3Cl5{N(CH3)[Si(CH3)3]}

2007 ◽  
Vol 72 (10) ◽  
pp. 1407-1419 ◽  
Author(s):  
Radka Voznicová ◽  
Milan Alberti ◽  
Jan Taraba ◽  
Dalibor Dastych ◽  
Pavel Kubáček ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Experimental Data ◽  
Dft Calculations ◽  
Crystal Structures ◽  
Elemental Analysis ◽  
Molar Ratio ◽  
Monoclinic Space Group ◽  
X Ray Diffraction ◽  
X Ray ◽  
Molecular And Crystal Structures

The reaction of P3N3Cl6 (1) with heptamethyldisilazane in the molar ratio 1:1 leads to the formation of 2,4,4,6,6-pentachloro-N-methyl-N-(trimethylsilyl)cyclotriphosphazen-2-amine, P3N3Cl5{N(CH3)[Si(CH3)3]} (2). Compound 2 was characterized by elemental analysis and spectroscopically. Molecular and crystal structures of 2 were determined by X-ray diffraction. 2 is monoclinic, space group P21/n. Experimental data were compared with results of DFT calculations.

Vibrational spectroscopy and crystal structure analysis of two polymorphs of the di-amino acid peptide cyclo(L -Glu-L -Glu)

2009 ◽  
Vol 41 (3) ◽  
pp. 288-302 ◽  
Author(s):  
Andrew P. Mendham ◽  
Rex A. Palmer ◽  
Brian S. Potter ◽  
Trevor J. Dines ◽  
Martin J. Snowden ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Structure Analysis ◽  
Vibrational Spectroscopy ◽  
Crystal Structure Analysis ◽  
Amino Acid Peptide

7-Azaindole-3-carboxylic acid and its Pt(II) and Pd(II) complexes: Crystal structure of the ligand, vibrational spectra, DFT calculations and in vitro antiproliferative activity

2020 ◽  
Vol 1203 ◽  
pp. 127441 ◽  
Author(s):  
Ksenia Szmigiel-Bakalarz ◽  
Markus Nentwig ◽  
Oliver Oeckler ◽  
Magdalena Malik-Gajewska ◽  
Beata Filip-Psurska ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Carboxylic Acid ◽  
Dft Calculations ◽  
Vibrational Spectra ◽  
Antiproliferative Activity

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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