scholarly journals A pH-dependent structural transition in the homopurine-homopyrimidine tract in superhelical DNA

1986 ◽  
Vol 2 (3) ◽  
pp. 115-124 ◽  
Author(s):  
V. I. Lyamichev ◽  
S. M. Mirkin ◽  
M. D. Frank-Kamenetskii
Keyword(s):  
Structural Transition ◽  
Ph Dependent

pH-dependent size and structural transition in P123 micelle induced gold nanoparticles

RSC Advances ◽  
2015 ◽  
Vol 5 (85) ◽  
pp. 69765-69775 ◽  
Author(s):  
P. Chatterjee ◽  
S. Hazra
Keyword(s):  
Gold Nanoparticles ◽  
Structural Transition ◽  
Ph Value ◽  
Ph Dependent

The transition of the structure and size of AuNPs at a pH value around 9.5, from slowly grown, well-faceted, large (≫19 nm), less uniform and near connected to fast grown, near symmetrical, small (<19 nm), more uniform and well-separated, is observed.

Molecular Basis for the pH Dependent Structural Transition of Nitrophorin 4

2009 ◽  
Vol 113 (7) ◽  
pp. 2135-2142 ◽  
Author(s):  
Marcelo A. Martí ◽  
Dario A. Estrin ◽  
Adrián E. Roitberg
Keyword(s):  
Molecular Basis ◽  
Structural Transition ◽  
Nitrophorin 4 ◽  
Ph Dependent

pH-dependent permeability change and reversible structural transition of PEGylated polyion complex vesicles (PICsomes) in aqueous media

Soft Matter ◽  
2009 ◽  
Vol 5 (3) ◽  
pp. 529-532 ◽  
Author(s):  
Akihiro Kishimura ◽  
Sittipong Liamsuwan ◽  
Hiroyuki Matsuda ◽  
Wen-Fei Dong ◽  
Kensuke Osada ◽  
...  
Keyword(s):  
Structural Transition ◽  
Aqueous Media ◽  
Permeability Change ◽  
Polyion Complex ◽  
Ph Dependent

Elucidating the pH-Dependent Structural Transition of T7 Bacteriophage Endolysin

Biochemistry ◽  
2016 ◽  
Vol 55 (33) ◽  
pp. 4614-4625 ◽  
Author(s):  
Meenakshi Sharma ◽  
Dinesh Kumar ◽  
Krishna Mohan Poluri
Keyword(s):  
Structural Transition ◽  
Ph Dependent ◽  
T7 Bacteriophage ◽  
Bacteriophage Endolysin

scholarly journals pH-dependent structural transition in rabbit skeletal troponin C.

1987 ◽  
Vol 262 (20) ◽  
pp. 9636-9640
Author(s):  
C L Wang ◽  
Q Zhan ◽  
T Tao ◽  
J Gergely
Keyword(s):  
Structural Transition ◽  
Troponin C ◽  
Ph Dependent

The Reaction of Thiol Compounds with the Vitamin-K Dependent Clotting Factors

1969 ◽  
Vol 21 (03) ◽  
pp. 573-579 ◽  
Author(s):  
P Fantl
Keyword(s):  
Prothrombin Time ◽  
Vitamin K ◽  
Anaerobic Conditions ◽  
Clotting Factors ◽  
Thiol Compounds ◽  
Aerobic Conditions ◽  
One Stage ◽  
Factor Ii ◽  
Ph Dependent ◽  
The One

SummaryTreatment of human and dog oxalated plasma with 0.2 to 1.0 × 10−1 M 2.3-dithiopropanol (BAL) or dithiothreitol (DTT) at 2–4° C for 30 min results in the reduction of the vitamin-K dependent clotting factors II, VII, IX and X to the respective-SH derivatives. The reaction is pH dependent. Under aerobic conditions the delayed one stage prothrombin time can be partly reversed. Under anaerobic conditions a gradual prolongation of the one stage prothrombin time occurs without reversal.In very diluted plasma treated with the dithiols, prothrombin can be converted into thrombin if serum as source of active factors VII and X is added. In contrast SH factors VII, IX and X are inactive in the specific tests. Reoxidation to active factors II, VII, IX and X takes place during adsorption and elution of the SH derivatives. The experiments have indicated that not only factor II but also factors VII, IX and X have active-S-S-centres.

Rationalizing the pH-Activity Response for Escherichia Coli’s Glycinamide Ribonucleotidetransformylase Through Computational Methods

2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta
Keyword(s):  
Transfer Reaction ◽  
Catalytic Mechanism ◽  
Ph Dependence ◽  
Ph Effects ◽  
Dependent Manner ◽  
E Coli ◽  
Gar Tfase ◽  
Activity Curve ◽  
Ph Dependent ◽  
Formyl Transfer

<div>Human Glycinamide ribonucleotide transformylase (GAR Tfase), a regulatory enzyme in the de novo purine biosynthesis pathway, has been established as an anti-cancer target. GAR Tfase catalyzes the formyl transfer reaction from the folate cofactor to the GAR ligand. In the present work, we study E. coli GAR Tfase, which has high sequence similarity with the human GAR Tfase with most functional residues conserved. E. coli GAR Tfase exhibits structural changes and the binding of ligands that varies with pH which leads to change the rate of the formyl transfer reaction in a pH-dependent manner. Thus, the inclusion of pH becomes essential for the study of its catalytic mechanism. Experimentally, the pH-dependence of the kinetic parameter kcat is measured to evaluate the pH-range of enzymatic activity. However, insufficient information about residues governing the pH-effects on the catalytic activity leads to ambiguous assignments of the general acid and base catalysts and consequently its catalytic mechanism. In the present work, we use pH-replica exchange molecular dynamics (pH-REMD) simulations to study the effects of pH on E. coli GAR Tfase enzyme. We identify the titratable residues governing the pH-dependent conformational changes in the system. Furthermore, we filter out the protonation states which are essential in maintaining the structural integrity, keeping the ligands bound and assisting the catalysis. We reproduce the experimental pH-activity curve by computing the population of key protonation states. Moreover, we provide a detailed description of residues governing the acidic and basic limbs of the pH-activity curve.</div>

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