Two-dimensional wave regimes in a thin layer of a viscous fluid

1985 ◽  
Vol 20 (3) ◽  
pp. 389-394 ◽  
Author(s):  
E. A. Demekhin ◽  
V. Ya. Shkadov
Keyword(s):  
Viscous Fluid ◽  
Thin Layer ◽  
Two Dimensional ◽  
Dimensional Wave

An advanced experimental investigation of quasi-two-dimensional shear flow

1992 ◽  
Vol 241 ◽  
pp. 705-722 ◽  
Author(s):  
F. V. Dolzhanskii ◽  
V. A. Krymov ◽  
D. Yu. Manin
Keyword(s):  
Experimental Investigation ◽  
Shear Flow ◽  
Viscous Fluid ◽  
Thin Layer ◽  
Driving Force ◽  
Flow Characteristics ◽  
Vortical Flow ◽  
Two Dimensional ◽  
Dimensional Approximation ◽  
The Stability

Forced shear flows in a thin layer of an incompressible viscous fluid are studied experimentally. Streak photographs are used to obtain the stream function of vortical flow patterns arising after the primary shear flow loses stability. Various flow characteristics are determined and results are compared to the stability theory of quasi-two-dimensional flows. The applicability of the quasi-two-dimensional approximation is directly verified and the possibility of reconstruction of the driving force from the secondary flow pattern is demonstrated.

scholarly journals Studies on the autophosphorylation of the insulin receptor from human placenta. Analysis of the sites phosphorylated by two-dimensional peptide mapping

1988 ◽  
Vol 252 (2) ◽  
pp. 607-615 ◽  
Author(s):  
J M Tavaré ◽  
R M Denton
Keyword(s):  
Thin Layer ◽  
Insulin Receptor ◽  
Peptide Mapping ◽  
Beta Subunit ◽  
Two Dimensional ◽  
Intact Cells ◽  
Tyrosine Residues ◽  
Domain 3 ◽  
Receptor Beta

1. A partially purified preparation of human placental insulin receptors was incubated with [gamma-32P]ATP in the presence or absence of insulin. The 32P-labelled insulin-receptor beta-subunits were then isolated, cleaved with trypsin followed by protease V8 and the [32P]phosphopeptides generated were analysed by thin layer electrophoresis and chromatography. This approach revealed that insulin stimulates autophosphorylation of the insulin-receptor beta-subunit in vitro on at least seven tyrosine residues distributed among three distinct domains. 2. One domain (domain 2), containing tyrosine residues 1146, 1150 and 1151 was the most rapidly phosphorylated and could be recovered as mono-, di- and triphosphorylated peptides cleaved by trypsin at Arg-1143 and either Lys-1153 or Lys-1156. Multiple phosphorylation of this domain appears to partially inhibit the cleavage at Lys-1153 by trypsin. 3. In a second domain (domain 3) containing two phosphorylated tyrosine residues at positions 1316 and 1322 the tyrosines were phosphorylated more slowly than those in domain 2. This domain is close to the C-terminus of the beta-subunit polypeptide chain. 4. At least two further tyrosine residues appeared to be phosphorylated after those in domains 2 and 3. These residues probably residue within a domain lying in close proximity to the inner face of the plasma membrane containing tyrosines 953, 960 and 972, but conclusive evidence is still required. 5. The two-dimensional thin-layer analysis employed in this study to investigate insulin-receptor phosphorylation has several advantages over previous methods based on reverse-phase chromatography. It allows greater resolution of 32P-labelled tryptic peptides and, when coupled to radioautography, is considerably more sensitive. The approach can be readily adapted to study phosphorylation of the insulin receptor within intact cells.

Diffraction of a pulse by a resistive half-plane. I. Normal incidence

1960 ◽  
Vol 255 (1283) ◽  
pp. 538-549 ◽  
Keyword(s):  
Time Dependence ◽  
Half Plane ◽  
Wave Diffraction ◽  
Diffraction Problem ◽  
Normal Incidence ◽  
Step Function ◽  
Two Dimensional ◽  
Dynamic Similarity ◽  
Function Time ◽  
Dimensional Wave

The two-dimensional wave diffraction problem, acoustic or electromagnetic, in which a pulse of step-function time dependence is diffracted by a resistive half-plane is solved by assuming dynamic similarity in the solution.

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