X-ray diffraction of a cysteine-containing bacteriorhodopsin mutant and its mercury derivative. Localization of an amino acid residue in the loop of an integral membrane protein

Biochemistry ◽  
1993 ◽  
Vol 32 (47) ◽  
pp. 12830-12834 ◽  
Author(s):  
Mark P. Krebs ◽  
Wolfgang Behrens ◽  
Ramin Mollaaghababa ◽  
H. Gobind Khorana ◽  
Maarten P. Heyn
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Amino Acid Residue ◽  
Integral Membrane Protein ◽  
X Ray Diffraction ◽  
X Ray ◽  
Mercury Derivative

X-ray diffraction analysis of matrix porin, an integral membrane protein from Escherichia coli outer membranes

1983 ◽  
Vol 164 (2) ◽  
pp. 313-327 ◽  
Author(s):  
R.M. Garavito ◽  
J. Jenkins ◽  
J.N. Jansonius ◽  
R. Karlsson ◽  
J.P. Rosenbusch
Keyword(s):  
Escherichia Coli ◽  
Membrane Protein ◽  
Diffraction Analysis ◽  
Integral Membrane Protein ◽  
X Ray Diffraction ◽  
X Ray ◽  
Outer Membranes

C−H⋅⋅⋅O Hydrogen Bond Mediated Chain Reversal in a Peptide Containing aγ-Amino Acid Residue, Determined Directly from Powder X-ray Diffraction Data

2002 ◽  
Vol 114 (3) ◽  
pp. 512-514 ◽  
Author(s):  
Eugene Y. Cheung ◽  
Emma E. McCabe ◽  
Kenneth D. M. Harris ◽  
Roy L. Johnston ◽  
Emilio Tedesco ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Diffraction Data ◽  
X Ray Diffraction ◽  
X Ray ◽  
Chain Reversal

Axially Chiral Bis(α-amino Acid)s and Their Deamino Analogues. Synthesis and Configurational Assignment

1998 ◽  
Vol 63 (2) ◽  
pp. 211-221 ◽  
Author(s):  
Miloš Tichý ◽  
Luděk Ridvan ◽  
Miloš Buděšínský ◽  
Jiří Závada ◽  
Jaroslav Podlaha ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nmr Spectra ◽  
Building Blocks ◽  
X Ray Diffraction ◽  
Amino Groups ◽  
X Ray ◽  
Configurational Assignment ◽  
Symmetry Properties ◽  
Axially Chiral ◽  
Polymeric Structures

The axially chiral bis(α-amino acid)s cis-2 and trans-2 as possible building blocks for polymeric structures of novel type of helicity were prepared. Their configuration has been determined by NMR spectroscopy and, in the case of the trans-isomer, confirmed by single-crystal X-ray diffraction. Analogous pair of stereoisomeric diacids cis-3 and trans-3, devoid of the amino groups, was also prepared and their configuration assigned. The observed differences in the NMR spectra of cis- and trans-isomers of 2 and 3 are discussed from the viewpoint of their different symmetry properties.

Crystallization and preliminary X-ray analysis of ferric enterobactin receptor FepA, an integral membrane protein fromEscherichia coli

1998 ◽  
Vol 54 (4) ◽  
pp. 697-699 ◽  
Author(s):  
Barbara S. Smith ◽  
Bostjan Kobe ◽  
Ravi Kurumbail ◽  
Susan K. Buchanan ◽  
Lalitha Venkatramani ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
X Ray ◽  
Fromescherichia Coli

scholarly journals Synthesis, characterization, x-ray diffraction studies and biological activities of iron(III) and cobalt(II) complexes with alanine

2018 ◽  
Vol 6 (2) ◽  
pp. 132
Author(s):  
Shuaibu Musa ◽  
S O. Idris ◽  
A D. Onu
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Human Life ◽  
Molar Conductance ◽  
Biological Molecules ◽  
X Ray Diffraction ◽  
Monoclinic Crystal ◽  
X Ray ◽  
Metal Ligands ◽  
Elemental Analyses

The resulted complexes produced between Fe (III) and Co (II) with biological molecules like amino acids play an important role in human life. They can be used as bioactive compounds as well as in industries. Fe (III) and Co (II) complexes are synthesized with Alanine amino acid. The complexes were characterized by X-ray diffraction, magnetic suscetivility, elemental analysis (AAS), molar conductance, melting point, infrared and uv-visible spectrophotometry analyses. The elemental analyses were used to determine the chelation ratio, 1:3(metal: ligands) for iron (III) Alanine and 1:2 ratio for cobalt (II) Alanine. The molar conductivity of the complexes show that the complexes are not electrolytic in nature. The x-ray data suggest monoclinic crystal system for all the complexes with the exception of Co-alanine, which is hexagonal. The magnetic susceptivility and electronic spectra suggest the complexes are high spin with octahedral geometry.The complexes show enhance activity in comparable to the amino acid.  

scholarly journals HUMAN AMYLOID PROTEIN: CHEMICAL VARIABILITY AND HOMOGENEITY

1971 ◽  
Vol 19 (1) ◽  
pp. 1-15 ◽  
Author(s):  
M. HARADA ◽  
C. ISERSKY ◽  
P. CUATRECASAS ◽  
D. PAGE ◽  
H. A. BLADEN ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amyloid Fibril ◽  
Gel Filtration ◽  
Protein S ◽  
Amyloid Protein ◽  
X Ray Diffraction ◽  
Amyloid Proteins ◽  
X Ray ◽  
Chemical Variability ◽  
Sepharose 4B

The morphology of the fibril of amyloid derived from different individuals is similar, but occasionally significant differences are noted. All human amyloid filaments have a "β-pleated sheet" conformation as revealed by x-ray diffraction, and those examined after orientation show a "cross-β" pattern. All amyloid fibril concentrates studied so far can be fractionated to obtain the major amyloid protein component(s) by sequential gel filtration with 5 M guanidine-HCl in 1 N acetic acid on Sepharose 4B and Sephadex G-100 or G-75 columns with the removal of over 28% of proteins representing minor constituents. The major amyloid protein(s) obtained from the spleen and/or liver of six patients is found to contain tryptophan, to be deficient in hydroxylysine and hydroxyproline and usually at least one commonly occurring amino acid and to have a high content of dicarboxylic acid and short chain amino acids and unreactive (blocked) NH2-terminal groups or aspartic acid-asparagine (Asx). However, the amyloid protein(s) from each individual differs from that of the others in molecular weight, in amino acid composition and in the presence or absence of specific tryptic peptides. Amyloid protein(s) from the liver and spleen of the same individual is identical. No chemical characteristics distinguish amyloid proteins derived from cases classified clinically as "primary" from those classified as "secondary." There is a striking chemical similarity between amyloid proteins and the NH2-terminal variable fragment of the light and heavy chain of immumoglobulin proteins.

Elucidation of the two-dimensional structure of an α-amino acid surfactant monolayer on water using synchrotron X-ray diffraction

Nature ◽  
1987 ◽  
Vol 328 (6125) ◽  
pp. 63-66 ◽  
Author(s):  
Sharon Grayer Wolf ◽  
Leslie Leiserowitz ◽  
Meir Lahav ◽  
Moshe Deutsch ◽  
Kristian Kjaer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dimensional Structure ◽  
Two Dimensional ◽  
X Ray Diffraction ◽  
X Ray
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