A computational study of thiol-containing cysteine amino acid binding to Au6 and Au8 gold clusters

2020 ◽  
Vol 26 (3) ◽  
Author(s):  
Pham Vu Nhat ◽  
Pham Tran Nguyen Nguyen ◽  
Nguyen Thanh Si
2021 ◽  
Vol 125 (16) ◽  
pp. 3244-3256
Author(s):  
Pham Vu Nhat ◽  
Nguyen Thanh Si ◽  
Nguyen Thanh Tien ◽  
Minh Tho Nguyen

1991 ◽  
Vol 266 (34) ◽  
pp. 23135-23141 ◽  
Author(s):  
W. Schlumbohm ◽  
T. Stein ◽  
C. Ullrich ◽  
J. Vater ◽  
M. Krause ◽  
...  

2014 ◽  
Vol 38 ◽  
pp. 101-106 ◽  
Author(s):  
Xuefang Shang ◽  
Jinge Du ◽  
Wancai Yang ◽  
Yun Liu ◽  
Zhiyuan Fu ◽  
...  

2019 ◽  
Vol 43 (4) ◽  
Author(s):  
Listya Purnamasari ◽  
Ali Agus ◽  
Cuk Tri Noviandi

This research aimed to observe the interaction of methionine-cysteine amino acid supplementation to decrease the effect of aflatoxin B1 (AFB1) on diet against production performance of broiler chicken. A number of 240 mixed sex broiler chickens were treated in 9 treatments by factorial design 3 x 3 with methionine-cysteine amino acid (M+C) (75,100, dan 125%) factors and AFB1 levels (0, 200, dan 400 ppb). Variables observed were: Weight gain, feed consumption, and feed conversion ratio (FCR). The results showed that increased AFB1 content in diet from 0 to 400 ppb increased chicken body weight (P <0.05) in each age group. The high body weight was balanced with high feed consumption along with increased nutrient needs, mainly sulfuric amino acid (M+C) as the precursor of glutathione to eliminate toxic through conjugation reactions. The interaction effect was firstly occurred between M + C and AFB1 treatment (P <0.05). Meanwhile increased supplementation of M + C from 75 to 125% caused decreased feed consumption in each age group of chickens, but increased AFB1 levels further increased feed consumption (P<0.05). The interaction effect between the level of M + C and AFB1 contamination in diets on feed consumption were seen in 21-day-old chickens (P<0.05). FCR was also increased (P <0.05) with the reduction of M + C content in diet at 7 days old. The effect of AFB1 on diet and interaction between M + C and AFB1 on chicken FCR in this study was not significant in all age groups. It can be concluded from the current study that supplying methionine-cystine amino acid with 75, 100 and 125% in AFB1 contaminated diet of 0, 200 and 400 ppb improves the performance of broiler chicken production.


2006 ◽  
Vol 361 (1474) ◽  
pp. 1751-1760 ◽  
Author(s):  
William R Taylor

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.


1990 ◽  
Vol 53 (4) ◽  
pp. 314-320 ◽  
Author(s):  
J B Penney ◽  
W F Maragos ◽  
J T Greenamyre ◽  
D L Debowey ◽  
Z Hollingsworth ◽  
...  

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

2017 ◽  
Vol 37 (4) ◽  
Author(s):  
Yu-Xing Lu ◽  
Xin-Xin Liu ◽  
Wei-Bing Liu ◽  
Bang-Ce Ye

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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