In vivo and in vitro protein mediated synthesis of palladium nanoparticles for hydrogenation reactions

2020 ◽  
Vol 56 (76) ◽  
pp. 11211-11214
Author(s):  
Oren Bachar ◽  
Matan Moshe Meirovich ◽  
Ronni Kurzion ◽  
Omer Yehezkeli
Keyword(s):  
Palladium Nanoparticles ◽  
Ethylene Conversion ◽  
Hydrogenation Reactions ◽  
Vitro Protein

We report the biosynthesis of size confined palladium nanoparticles (Pd-NPs) in bacteria that can be utilized for acetylene to ethylene conversion while maintaining viability.

Applicability of Instability Index for In vitro Protein Stability Prediction

2019 ◽  
Vol 26 (5) ◽  
pp. 339-347 ◽  
Author(s):  
Dilani G. Gamage ◽  
Ajith Gunaratne ◽  
Gopal R. Periyannan ◽  
Timothy G. Russell
Keyword(s):  
Protein Stability ◽  
Caulobacter Crescentus ◽  
Effect Of Temperature ◽  
Instability Index ◽  
Dipeptide Composition ◽  
Experimental Conditions ◽  
The Stability ◽  
Vitro Protein

Background: The dipeptide composition-based Instability Index (II) is one of the protein primary structure-dependent methods available for in vivo protein stability predictions. As per this method, proteins with II value below 40 are stable proteins. Intracellular protein stability principles guided the original development of the II method. However, the use of the II method for in vitro protein stability predictions raises questions about the validity of applying the II method under experimental conditions that are different from the in vivo setting. Objective: The aim of this study is to experimentally test the validity of the use of II as an in vitro protein stability predictor. Methods: A representative protein CCM (CCM - Caulobacter crescentus metalloprotein) that rapidly degrades under in vitro conditions was used to probe the dipeptide sequence-dependent degradation properties of CCM by generating CCM mutants to represent stable and unstable II values. A comparative degradation analysis was carried out under in vitro conditions using wildtype CCM, CCM mutants and two other candidate proteins: metallo-β-lactamase L1 and α -S1- casein representing stable, borderline stable/unstable, and unstable proteins as per the II predictions. The effect of temperature and a protein stabilizing agent on CCM degradation was also tested. Results: Data support the dipeptide composition-dependent protein stability/instability in wt-CCM and mutants as predicted by the II method under in vitro conditions. However, the II failed to accurately represent the stability of other tested proteins. Data indicate the influence of protein environmental factors on the autoproteolysis of proteins. Conclusion: Broader application of the II method for the prediction of protein stability under in vitro conditions is questionable as the stability of the protein may be dependent not only on the intrinsic nature of the protein but also on the conditions of the protein milieu.

scholarly journals In Vivo and In Vitro Protein Ligation by Naturally Occurring and Engineered Split DnaE Inteins

PLoS ONE ◽  
2009 ◽  
Vol 4 (4) ◽  
pp. e5185 ◽  
Author(s):  
A. Sesilja Aranko ◽  
Sara Züger ◽  
Edith Buchinger ◽  
Hideo Iwaï
Keyword(s):  
Protein Ligation ◽  
Naturally Occurring ◽  
Vitro Protein

Use of an in Vitro Protein Synthesizing System to Test the Mode of Action of Chloracetamides

Weed Science ◽  
1980 ◽  
Vol 28 (3) ◽  
pp. 334-340 ◽  
Author(s):  
Luanne M. Deal ◽  
J. T. Reeves ◽  
B. A. Larkins ◽  
F. D. Hess
Keyword(s):  
Protein Synthesis ◽  
Sand Culture ◽  
Leucine Incorporation ◽  
Insoluble Protein ◽  
In Vitro System ◽  
A Cell ◽  
Protein Incorporation ◽  
Vitro Protein

The effects of chloracetamides on protein synthesis were studied both in vivo and in vitro. Four chloracetamide herbicides, alachlor [2-chloro-2′,6′-diethyl-N-(methoxymethyl)acetanilide], metolachlor [2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-methoxy-1-methylethyl)acetamide], CDAA (N–N-diallyl-2-chloroacetamide), and propachlor (2-chloro-N-isopropylacetanilide) were tested for inhibition of [3H]-leucine incorporation into protein. Incorporation of3H-leucine into trichloroacetic acid (TCA)-insoluble protein was inhibited in oat (Avena sativaL. ‘Victory’) seedlings grown in sand culture and treated 12 h at 1 × 10−4M with these chloracetamides. The herbicides were also tested in a cell-free protein synthesizing system containing polyribosomes purified from oat root cytoplasm. These herbicides had no effect on the rates of polypeptide elongation nor on the synthesis of specific polypeptides when herbicides (1 × 10−4M) were added directly to the system. Polypeptide formation was inhibited 89% when 1 × 10−4M cycloheximide was added during translation. Cytoplasmic polyribosomes were isolated from oat roots treated 12 h with 1 × 10−4M herbicide. Translation rates and products were not altered when these polyribosomes were added to the in vitro system. Protein synthesis is inhibited when tested in an in vivo system; however, the inhibition does not occur during the translation of mRNA into protein.

scholarly journals Combining in vitro protein detection and in vivo antibody detection identifies potential vaccine targets against Staphylococcus aureus during osteomyelitis

2016 ◽  
Vol 206 (1) ◽  
pp. 11-22 ◽  
Author(s):  
P. Martijn den Reijer ◽  
Marjan Sandker ◽  
Susan V. Snijders ◽  
Mehri Tavakol ◽  
Antoni P. A. Hendrickx ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Protein Detection ◽  
Antibody Detection ◽  
Potential Vaccine ◽  
Vitro Protein

scholarly journals In vivo versus in vitro protein abundance analysis of Shigella dysenteriae type 1 reveals changes in the expression of proteins involved in virulence, stress and energy metabolism

2011 ◽  
Vol 11 (1) ◽  
pp. 147 ◽  
Author(s):  
Srilatha Kuntumalla ◽  
Quanshun Zhang ◽  
John C Braisted ◽  
Robert D Fleischmann ◽  
Scott N Peterson ◽  
...  
Keyword(s):  
Energy Metabolism ◽  
Shigella Dysenteriae ◽  
Protein Abundance ◽  
Shigella Dysenteriae Type ◽  
Vitro Protein

In vivo and in vitro protein solubility assays using split GFP

2006 ◽  
Vol 3 (10) ◽  
pp. 845-854 ◽  
Author(s):  
Stéphanie Cabantous ◽  
Geoffrey S Waldo
Keyword(s):  
Protein Solubility ◽  
Vitro Protein

PHENYLALANINE METABOLISM IN SHEEP INFUSED WITH GLUCOSE PLUS INSULIN. II. EFFECTS ON IN VIVO AND IN VITRO PROTEIN SYNTHESIS AND RELATED ENERGY EXPENDITURES

1988 ◽  
Vol 68 (3) ◽  
pp. 721-730 ◽  
Author(s):  
RICHARD J. EARLY ◽  
BRIAN W. McBRIDE ◽  
RONALD O. BALL
Keyword(s):  
Protein Synthesis ◽  
Gastrocnemius Muscle ◽  
Specific Radioactivity ◽  
Intercostal Muscle ◽  
Energy Expenditures ◽  
Phenylalanine Metabolism ◽  
Arterial Plasma ◽  
Vitro Protein

In vivo fractional rates of protein synthesis (FSR), based on both intracellular fluid (ICF) and arterial plasma specific radioactivity (SRA), were determined for the external intercostal muscle (EIC), gastrocnemius muscle, liver and kidneys of growing sheep during infusions of either saline or glucose (2 g h−1) plus insulin (1.2 U h−1; G+I). In vitro FSR and energy expenditures associated with protein synthesis (cycloheximide-sensitive respiration) and Na+, K+ transport (ouabain-sensitive respiration) were also determined in EIC muscle. In vivo FSR based on ICF SRA in muscle were not significantly different between G+I and S infused sheep (5.2 vs. 4.2% d−1 and 5.0 vs. 3.2% d−1 for EIC and gastrocnemius, respectively). In vivo FSR in the liver (54 vs. 61% d−1) and kidneys (38 vs. 55% d−1) were also not significantly different between G+I versus S infused sheep. Based on plasma SRA, FSR in all tissues were unaffected by treatments and were less (P < 0.05) than those calculated from ICF SRA. In vitro FSR and the energy expenditures associated with protein synthesis and Na+, K+ transport were not affected by G+I infusions. The average in vitro FSR in isolated EIC muscle (2.7% d−1) was 53% and 81% of the average in vivo FSR calculated from ICF and plasma SRA, respectively. Compared to data reported for nonruminants, these data suggest that rates of protein synthesis and energy expenditures associated with protein synthesis in ruminants are less influenced by insulin and glucose. Key words: Sheep, protein synthesis, insulin, glucose, Na+, K+ transport

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