The development and amino acid binding ability of nano-materials based on azo derivatives: Theory and experiment

2014 ◽  
Vol 38 ◽  
pp. 101-106 ◽  
Author(s):  
Xuefang Shang ◽  
Jinge Du ◽  
Wancai Yang ◽  
Yun Liu ◽  
Zhiyuan Fu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Nano Materials ◽  
Binding Ability ◽  
Azo Derivatives ◽  
Amino Acid Binding ◽  
Theory And Experiment

Thermal denaturation and amino acid binding ability of soluble RNA

1963 ◽  
Vol 10 (2) ◽  
pp. 117-121 ◽  
Author(s):  
M. Arcà ◽  
C. Calvori ◽  
L. Frontali ◽  
G. Tecce
Keyword(s):  
Amino Acid ◽  
Thermal Denaturation ◽  
Binding Ability ◽  
Amino Acid Binding

scholarly journals An active serine is involved in covalent substrate amino acid binding at each reaction center of gramicidin S synthetase.

1991 ◽  
Vol 266 (34) ◽  
pp. 23135-23141 ◽  
Author(s):  
W. Schlumbohm ◽  
T. Stein ◽  
C. Ullrich ◽  
J. Vater ◽  
M. Krause ◽  
...  
Keyword(s):  
Amino Acid ◽  
Reaction Center ◽  
Gramicidin S ◽  
Amino Acid Binding

scholarly journals Transcription and translation in an RNA world

2006 ◽  
Vol 361 (1474) ◽  
pp. 1751-1760 ◽  
Author(s):  
William R Taylor
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Rna World ◽  
Large Subunit ◽  
Trna Synthetase ◽  
Nucleoside Triphosphate ◽  
Amino Acid Binding ◽  
World Hypothesis ◽  
Protein Elongation ◽  
Rna World Hypothesis

The RNA world hypothesis requires a ribozyme that was an RNA-directed RNA polymerase (ribopolymerase). If such a replicase makes a reverse complementary copy of any sequence (including itself), in a simple RNA world, there is no mechanism to prevent self-hybridization. It is proposed that this can be avoided through the synthesis of a parallel complementary copy. The logical consequences of this are pursued and developed in a computer simulation, where the behaviour of the parallel copy is compared to the conventional reverse complementary copy. It is found that the parallel copy is more efficient at higher temperatures (up to 90°C). A model for the ribopolymerase, based on the core of the large subunit (LSU) of the ribosome, is described. The geometry of a potential active site for this ribopolymerase suggests that it contained a cavity (now occupied by the aminoacyl-tRNA) and that an amino acid binding in this might have ‘poisoned’ the ribopolymerase by cross-reacting with the nucleoside-triphosphate before polymerization could occur. Based on a similarity to the active site components of the class-I tRNA synthetase enzymes, it is proposed that the amino acid could become attached to the nascent RNA transcript producing a variety of aminoacylated tRNA-like products. Using base-pairing interactions, some of these molecules might cross-link two ribopolymerases, giving rise to a precursor of the modern ribosome. A hybrid dimer, half polymerase and half proto-ribosome, could account for mRNA translocation before the advent of protein elongation factors.

scholarly journals Excitatory amino acid binding sites in the hippocampal region of Alzheimer's disease and other dementias.

1990 ◽  
Vol 53 (4) ◽  
pp. 314-320 ◽  
Author(s):  
J B Penney ◽  
W F Maragos ◽  
J T Greenamyre ◽  
D L Debowey ◽  
Z Hollingsworth ◽  
...  
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Amino Acid ◽  
Binding Sites ◽  
Excitatory Amino Acid ◽  
Hippocampal Region ◽  
Amino Acid Binding

scholarly journals Autoradiographic localization of cerebellar excitatory amino acid binding sites in the mouse

Neuroscience ◽  
1987 ◽  
Vol 22 (3) ◽  
pp. 913-923 ◽  
Author(s):  
J.M.M. Olson ◽  
J.T. Greenamyre ◽  
J.B. Penney ◽  
A.B. Young
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Excitatory Amino Acid ◽  
Amino Acid Binding

scholarly journals Identification and characterization of two types of amino acid-regulated acetyltransferases in actinobacteria

2017 ◽  
Vol 37 (4) ◽  
Author(s):  
Yu-Xing Lu ◽  
Xin-Xin Liu ◽  
Wei-Bing Liu ◽  
Bang-Ce Ye
Keyword(s):  
Amino Acid ◽  
Feedback Regulation ◽  
Protein Acetylation ◽  
Post Translational Modifications ◽  
Act Domain ◽  
Amino Acid Binding ◽  
Amino Acid Sensing ◽  
And Function ◽  
Future Work ◽  
The Relationship

Abstract One hundred and fifty GCN5-like acetyltransferases with amino acid-binding (ACT)-GCN5-related N-acetyltransferase (GNAT) domain organization have been identified in actinobacteria. The ACT domain is fused to the GNAT domain, conferring amino acid-induced allosteric regulation to these protein acetyltransferases (Pat) (amino acid sensing acetyltransferase, (AAPatA)). Members of the AAPatA family share similar secondary structure and are divided into two groups based on the allosteric ligands of the ACT domain: the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former are mainly found in Streptomyces; the latter are distributed in other actinobacteria. We investigated the effect of Asn and Cys on the acetylation activity of Sven_0867 (SvePatA, from Streptomyces venezuelae DSM 40230) and Amir_5672 (AmiPatA, from Actinosynnema mirum strain DSM 43827), respectively, as well as the relationship between the structure and function of these enzymes. These findings indicate that the activity of PatA and acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in actinobacteria. Amino acid-sensing signal transduction in acetyltransferases may be a mechanism that regulates protein acetylation in response to nutrient availability. Future work examining the relationship between protein acetylation and amino acid metabolism will broaden our understanding of post-translational modifications (PTMs) in feedback regulation.

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