Inverted Hydration Layers on Bio-Magnesium Surfaces in the Initial Degradation Stage and their Influence on Adsorption of Amino Acid Analogues: The Metadynamics Simulations

Langmuir ◽  
2019 ◽  
Vol 35 (52) ◽  
pp. 17009-17015
Author(s):  
Yu Zhao ◽  
Chong Qiao ◽  
Zhe Fang ◽  
Hongyan Wang ◽  
Shijie Zhu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Analogues ◽  
Hydration Layers

Site Specific Incorporation of Amino Acid Analogues into Proteins In Vivo

2000 ◽  
Author(s):  
Anne K. Kowal ◽  
Caroline Kohrer ◽  
Uttam L. RajBhandary
Keyword(s):  
Amino Acid ◽  
Site Specific ◽  
Amino Acid Analogues

An Efficient Access to Conformationally Rigid Amino Acid Analogues with a Piperidine Skeleton

Synlett ◽  
2010 ◽  
Vol 2010 (10) ◽  
pp. 1501-1504 ◽  
Author(s):  
Günter Haufe ◽  
Nirupam Purkayastha
Keyword(s):  
Amino Acid ◽  
Efficient Access ◽  
Amino Acid Analogues

scholarly journals Properties of phosphoenolpyruvate carboxykinase (guanosine triphosphate) synthesized in hepatoma cells in the presence of amino acid analogues

1975 ◽  
Vol 146 (3) ◽  
pp. 585-593 ◽  
Author(s):  
S E Knowles ◽  
J M Gunn ◽  
L Reshef ◽  
R W Hanson ◽  
F J Ballard
Keyword(s):  
Amino Acid ◽  
Phosphoenolpyruvate Carboxykinase ◽  
Hepatoma Cells ◽  
Dibutyryl Cyclic Amp ◽  
Enzyme Degradation ◽  
Amino Acid Analogues ◽  
Enzyme Molecules ◽  
Natural Amino Acids

1. Phosphoenolpyruvate carboxykinase (GTP) was induced by a combination of dibutyryl cyclic AMP, theophyline and dexamethasone in Reuber H35 hepatoma cells under conditions where an amino acid in the medium was replaced by an appropriate analogue. 2. With canavanine replacing arginine or with 5-fluorotryptophan or 6-fluorotryptophan replacing tryptophan the induced enzyme had a lower catalytic activity-relative to antibody reactivity. 3. These aberrant enzyme molecules were heat-labile in vitro. 4. Measurements of enzyme degradation in vivo indicated that the canavanine-containing enzyme and the 6-fluorotryptophan-containing enzyme were degraded more rapidly than the enzyme containing all natural amino acids.

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