scholarly journals Kinetics of bond formation in cross-linked gelatin gels

2006 ◽  
Vol 125 (17) ◽  
pp. 174903 ◽  
Author(s):  
T. Abete ◽  
E. Del Gado ◽  
D. Hellio Serughetti ◽  
L. de Arcangelis ◽  
M. Djabourov ◽  
...  
Keyword(s):  
Bond Formation ◽  
Gelatin Gels ◽  
Kinetics Of

Kinetics of Coordinate Bond Formation. V. Kinetics of the Reaction P(CH3)3+BF3

1961 ◽  
Vol 34 (3) ◽  
pp. 715-717 ◽  
Author(s):  
G. B. Kistiakowsky ◽  
C. E. Klots
Keyword(s):  
Bond Formation ◽  
Coordinate Bond ◽  
Kinetics Of

scholarly journals Kinetics of T3-DNA Ligase-Catalyzed Phosphodiester Bond Formation Measured Using the α-Hemolysin Nanopore

ACS Nano ◽  
2016 ◽  
Vol 10 (12) ◽  
pp. 11127-11135 ◽  
Author(s):  
Cherie S. Tan ◽  
Jan Riedl ◽  
Aaron M. Fleming ◽  
Cynthia J. Burrows ◽  
Henry S. White
Keyword(s):  
Bond Formation ◽  
Dna Ligase ◽  
Phosphodiester Bond ◽  
Kinetics Of

Kinetics of prebiotic depsipeptide formation from the ester–amide exchange reaction

2016 ◽  
Vol 18 (41) ◽  
pp. 28441-28450 ◽  
Author(s):  
Sheng-Sheng Yu ◽  
Ramanarayanan Krishnamurthy ◽  
Facundo M. Fernández ◽  
Nicholas V. Hud ◽  
F. Joseph Schork ◽  
...  
Keyword(s):  
Kinetic Model ◽  
Exchange Reaction ◽  
Bond Formation ◽  
Amide Bond ◽  
Amide Bond Formation ◽  
Amide Exchange ◽  
Kinetics Of

In this work, we introduce a kinetic model to study the effectiveness of ester-mediated amide bond formation under prebiotic conditions.

Dissolution Kinetics of Tuff Rock and Mechanism of Chemical Bond Formation at the Interface with Cement Grout

1984 ◽  
Vol 44 ◽  
Author(s):  
R. I. A. Malek ◽  
D. M. Roy
Keyword(s):  
Chemical Bond ◽  
Bond Formation ◽  
Dissolution Kinetics ◽  
Interfacial Region ◽  
Phase Identification ◽  
Dissolution Studies ◽  
Chemical Bond Formation ◽  
Calcium Aluminosilicate ◽  
Xrd Studies ◽  
Kinetics Of

AbstractThe interaction of tuff rock and cement was studied to evaluate the effectiveness of sealing of tuff boreholes with cementitious grouts. Previous studies indicated chemical bond formation between tuff and cement. Dissolution studies were carried out on Topopah Spring member tuff and on tuff with cement. The results indicate the formation of calcium silicate and calcium aluminosilicate hydrates; phase identification is confirmed by XRD studies. The significance of the results obtained and their implications on properties of the interfacial region are included.

scholarly journals Formation and intracellular transport of a heterodimeric viral spike protein complex.

1991 ◽  
Vol 112 (2) ◽  
pp. 257-266 ◽  
Author(s):  
R Persson ◽  
R F Pettersson
Keyword(s):  
Disulfide Bond ◽  
Intracellular Transport ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Membrane Glycoproteins ◽  
Virus Particles ◽  
Viral Glycoproteins ◽  
Protein Disulfide ◽  
Kinetics Of ◽  
Intrachain Disulfide Bond

We have analyzed the heterodimerization and intracellular transport from the ER to the Golgi complex (GC) of two membrane glycoproteins of a bunyavirus (Uukuniemi virus) that matures by a budding process in the GC. The glycoproteins G1 and G2, which form the viral spikes, are cotranslationally cleaved in the ER from a 110,000-D precursor. Newly synthesized G1 was transported to the GC and incorporated into virus particles about 30-45 min faster than newly synthesized G2. Analysis of the kinetics of intrachain disulfide bond formation showed that G1 acquired its mature form within 10 min, while completion of disulfide bond formation of G2 required a considerably longer time (up to 60 min). During the maturation process, G2 was transiently associated with the IgG heavy chain binding protein for a longer time than G1. Protein disulfide isomerase also coprecipitated with antibodies against G1 and G2. In virus particles, G1 and G2 were present exclusively as heterodimers. Immunoprecipitation with monoclonal antibodies showed that heterodimerization occurred rapidly, probably in the ER, between newly made G1 and mature, dimerization competent G2. Taken together, our results show that these two viral glycoproteins have different maturation kinetics in the ER. We conclude that the apparent different kinetics of ER to GC transport of G1 and G2 is due to the different rates by which these proteins fold and become competent to enter into heterodimeric complexes prior to exit from the ER.

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