Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γn, (αγ)n and γγδγ sequences

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crystal Structures ◽  
Structural Characterization ◽  
Side Chains ◽  
Amino Acid Residues

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.

Characterization of SNP, a Novel Tissue- and Phase-Specific Nuclear Protein Expressed during the Proliferative Phase in the Oviduct of the Lizard Podarcis sicula Raf.

2000 ◽  
Vol 381 (7) ◽  
pp. 615-618
Author(s):  
Piera Quesada ◽  
Luigia Atorino ◽  
Augusto Parente ◽  
Francesca Del Vecchio Blanco ◽  
Antimo Di Maro ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nuclear Protein ◽  
Reproductive Period ◽  
Amino Acid Residues ◽  
Seasonal Growth ◽  
Podarcis Sicula ◽  
Molecular Weights ◽  
Specific Nuclear Protein

Abstract The amino acid sequence of a novel tissueand phasespecific nuclear protein (SNP) has been determined, after purification from the nuclei of the oviduct of the lizard Podarcis sicula Raf. during the reproductive period of the seasonal growth. SNP has a pI of 9.0 and contains 81 amino acid residues with a molecular weight of 9211.88 ± 0.09. It shows a bipartite organization as the first 40 amino acids contain all 8 cysteinyl residues, while the last 41 amino acids contain 16 prolyl residues. Two more components have also been identified and characterized, with the first 79 amino acids matching SNP and missing one or two residues at the Cterminus. They have thus been named [des(Ala[81]) SNP1] and [des(Lys[80]Ala[81]) SNP2], respectively. The molecular weights are 9140.21 ± 0.83 for [des(Ala[81]) SNP1] and 9011 ± 0.09 for [des(Lys[80]Ala[81]) SNP2].

Studies in Thiohydantoin Chemistry. II. C-Terminal Sequencing of Peptides

1996 ◽  
Vol 49 (5) ◽  
pp. 551 ◽  
Author(s):  
F Casagranda ◽  
BM Duggan ◽  
A Kirkpatrick ◽  
RL Laslett ◽  
JFK Wilshire
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Side Chains ◽  
Amino Acid Residues ◽  
The Common ◽  
Derivatives Of

An investigation has been carried out into the thiocyanate degradation (AcOH/Ac2O/HSCN) procedure as it relates to the C-terminal sequencing of peptides, particular emphasis being placed on the sequencing of amino acid residues containing sensitive or functional side chains. Attempted C-terminal sequencing of several serine- and threonine -containing peptides stopped at these particular residues, and did not proceed further. It is concluded that sequencing of most of the common amino acids is achievable but that significant problems will have to be overcome before routine sequencing of proline , serine, threonine, arginine , and, in particular, aspartic and glutamic acids can be claimed. The action of base on the thiohydantoin derivatives of N,S- diacetylcysteine and N,S- diacetyl-β-methylcysteine causes β-elimination of thioacetic S-acid to give the corresponding olefinic thiohydantoins.

scholarly journals Structural characterization of α-amino acid complexes of molybdates: a spectroscopic and DFT study

RSC Advances ◽  
2015 ◽  
Vol 5 (12) ◽  
pp. 9010-9018 ◽  
Author(s):  
Lorenzo Biancalana ◽  
Marco Bortoluzzi ◽  
Claudia Forte ◽  
Fabio Marchetti ◽  
Guido Pampaloni
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Aqueous Medium ◽  
Structural Characterization ◽  
Computational Study ◽  
Dft Study ◽  
Amino Acid Complexes

A joint spectroscopic and computational study has allowed us to determine the dinuclear structural core of the products of the reactions between molybdates and α-amino acids in aqueous medium.

New hydrophobicL-amino acid salts: maleates ofL-leucine,L-isoleucine andL-norvaline

2015 ◽  
Vol 71 (7) ◽  
pp. 584-592 ◽  
Author(s):  
Sergey G. Arkhipov ◽  
Denis A. Rychkov ◽  
Alexey M. Pugachev ◽  
Elena V. Boldyreva
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Second Harmonic Generation ◽  
Crystal Structures ◽  
Harmonic Generation ◽  
Second Harmonic ◽  
Side Chains ◽  
Hydrophobic Amino Acid ◽  
Amino Acid Salts ◽  
Acid Salts

Crystals of maleates of three amino acids with hydrophobic side chains [L-leucenium hydrogen maleate, C6H14NO2+·C4H3O4−, (I), L-isoleucenium hydrogen maleate hemihydrate, C6H14NO2+·C4H3O4−·0.5H2O, (II), and L-norvalinium hydrogen maleate–L-norvaline (1/1), C5H11NO2+·C4H3O4−·C5H12NO2, (III)], were obtained. The new structures containC22(12) chains, or variants thereof, that are a common feature in the crystal structures of amino acid maleates. The L-leucenium salt is remarkable due to a large number of symmetrically non-equivalent units (Z′ = 3). The L-isoleucenium salt is a hydrate despite the fact that L-isoleucine is a nonpolar hydrophobic amino acid (previously known amino acid maleates formed hydrates only with lysine and histidine, which are polar and hydrophilic). The L-norvalinium salt provides the first example where the dimeric cation L-Nva...L-NvaH+was observed. All three compounds have layered noncentrosymmetric structures. Preliminary tests have shown the presence of the second harmonic generation (SGH) effect for all three compounds.

scholarly journals Cloning and characterization of the cDNA coding for a polymyositis-scleroderma overlap syndrome-related nucleolar 100-kD protein.

1992 ◽  
Vol 176 (4) ◽  
pp. 973-980 ◽  
Author(s):  
M Blüthner ◽  
F A Bautz
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Sequence ◽  
Epitope Mapping ◽  
Consensus Sequence ◽  
Overlap Syndrome ◽  
Amino Acid Residues ◽  
Protein Sequence Analysis ◽  
Protein Fragment

About 50% of patients with the polymyositis-scleroderma overlap syndrome are reported to have autoantibodies to a nucleolar particle termed PM/Scl. The particle consists of several polypeptides of which two proteins of 75 and 100 kD have been identified as the major antigenic components. Here we report on the cDNA cloning and partial epitope mapping of the 100-kD autoantigen from human placenta and HeLa lambda gt11 libraries. The deduced amino acid sequence encodes a protein of 885 amino acid residues with a molecular mass of 100.8 kD. Rabbit antibodies raised against a recombinant protein fragment reacted in immunofluorescence and immunoblotting in the same manner as human autoantibodies directed against the nucleolar 100-kD protein. Sequence analysis shows close homology to a consensus sequence of 12 amino acids from serine/threonine kinases, suggesting a possible function for this autoantigen. A major antigenic region is found to be located within the NH2-terminal third of the polypeptide.

scholarly journals Avoided motifs: short amino acid strings missing from protein datasets

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Pablo Mier ◽  
Miguel A. Andrade-Navarro
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Function ◽  
Large Protein ◽  
New Approach ◽  
Cellular Context ◽  
Human Proteins ◽  
Context Specific ◽  
Protein Datasets

Abstract According to the amino acid composition of natural proteins, it could be expected that all possible sequences of three or four amino acids will occur at least once in large protein datasets purely by chance. However, in some species or cellular context, specific short amino acid motifs are missing due to unknown reasons. We describe these as Avoided Motifs, short amino acid combinations missing from biological sequences. Here we identify 209 human and 154 bacterial Avoided Motifs of length four amino acids, and discuss their possible functionality according to their presence in other species. Furthermore, we determine two Avoided Motifs of length three amino acids in human proteins specifically located in the cytoplasm, and two more in secreted proteins. Our results support the hypothesis that the characterization of Avoided Motifs in particular contexts can provide us with information about functional motifs, pointing to a new approach in the use of molecular sequences for the discovery of protein function.

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