Migration of protons in a chain of tyrosine residues

2001 ◽  
Vol 84 (4) ◽  
pp. 409-415 ◽  
Author(s):  
V. E. Stefanov ◽  
A. A. Tulub
Keyword(s):  
Tyrosine Residues ◽  
A Chain

scholarly journals Chemical properties of the functional groups of insulin

1981 ◽  
Vol 193 (2) ◽  
pp. 419-425 ◽  
Author(s):  
Y K Chan ◽  
G Oda ◽  
H Kaplan
Keyword(s):  
Functional Groups ◽  
Chemical Properties ◽  
Amino Group ◽  
Histidine Residues ◽  
Tyrosine Residues ◽  
Order Of Magnitude ◽  
Phenolic Group ◽  
Dimeric Form ◽  
A Chain ◽  
Phenylalanine Residue

The method of competitive binding [Kaplan, Stevenson & Hartley (1971) Biochem. J. 124, 289-299] with 1-fluoro-2,4-dinitrobenzene as the labelling reagent [Duggleby & Kaplan (1975) Biochemistry 14, 5168-5175] was used to determine the chemical properties, namely pK and reactivity, of the amino groups, the histidine residues and the tyrosine residues of the dimeric form of pig zinc-free insulin at 20.0 degrees C. The N-terminal glycine residue of the A-chain has a pK of 7.7 and a slightly higher than normal reactivity. The N-terminal phenylalanine residue of the B-chain has a pK of 6.9 and is approximately an order of magnitude more reactive than a corresponding amino group with the same pK value. The lysine epsilon-amino group has an unusually low pK of 7.0 but has approximately the expected reactivity of such a group. In the case of the two histidine and four tyrosine residues only the average properties of each class were determined. The histidine residues have a pK value of approx. 6.6, but, however, their reactivity is at least an order of magnitude greater than that of a free imidazole group. The tyrosine residues have a pK value of approx. 10, but their average reactivities are substantially less than for a free phenolic group. At alkaline pH values above 8 the reactivity of all the functional groups show sharp discontinuities, indicating that insulin is undergoing a structural change that alters the properties of these groups.

scholarly journals The effect of iodination of particular tyrosine residues on the hormonal activity of insulin

1972 ◽  
Vol 126 (1) ◽  
pp. 123-131 ◽  
Author(s):  
C. J. Garratt ◽  
D. M. Harrison ◽  
Margaret Wicks
Keyword(s):  
Receptor Site ◽  
Target Tissue ◽  
Tyrosine Residue ◽  
Hormonal Activity ◽  
Tyrosine Residues ◽  
A Chain ◽  
The Individual ◽  
Adipose Cells

Insulin dissolved in aqueous or methanolic buffer was iodinated to give preparations containing an average of between one and five iodine atoms per insulin monomer. The resultant preparations were fragmented in various ways and the ratio of tyrosine to monoiodotyrosine and di-iodotyrosine was determined in each fragment. This has allowed the distribution of iodine between the combined A-chain tyrosine residues and the individual B-chain tyrosine residues to be determined. The hormonal activity of each of these iodinated insulin preparations was measured from their effect on the production of 14CO2 from [1-14C]glucose by isolated adipose cells. The results were interpreted as meaning that the iodination of tyrosine residue A19 or B16 leads to the inactivation of insulin. Speculations are made about the nature of an interaction between insulin and a receptor site on the target tissue.

Observation of Atom Rows in Thorium Pyromellitate Using a Field Emission STEM

1977 ◽  
Vol 35 ◽  
pp. 80-81
Author(s):  
H. Todokoro ◽  
S. Nomura ◽  
T. Komoda
Keyword(s):  
Field Emission ◽  
Amorphous Carbon ◽  
Carbon Film ◽  
Dark Field Image ◽  
Dark Field ◽  
Amorphous Carbon Film ◽  
Atomic Size ◽  
Wide Range ◽  
A Chain

It is interesting to observe polymers at atomic size resolution. Some works have been reported for thorium pyromellitate by using a STEM (1), or a CTEM (2,3). The results showed that this polymer forms a chain in which thorium atoms are arranged. However, the distance between adjacent thorium atoms varies over a wide range (0.4-1.3nm) according to the different authors.The present authors have also observed thorium pyromellitate specimens by means of a field emission STEM, described in reference 4. The specimen was prepared by placing a drop of thorium pyromellitate in 10-3 CH3OH solution onto an amorphous carbon film about 2nm thick. The dark field image is shown in Fig. 1A. Thorium atoms are clearly observed as regular atom rows having a spacing of 0.85nm. This lattice gradually deteriorated by successive observations. The image changed to granular structures, as shown in Fig. 1B, which was taken after four scanning frames.

Time-Resolved Cryo-Electron Microscopy of Oscillating Microtubules

1990 ◽  
Vol 48 (1) ◽  
pp. 502-503
Author(s):  
Eva-Maria Mandelkow ◽  
Ron Milligan
Keyword(s):  
Electron Microscopy ◽  
Dynamic Instability ◽  
Entire Solution ◽  
Reaction Scheme ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
A Chain ◽  
Ray Scattering

Microtubules form part of the cytoskeleton of eukaryotic cells. They are hollow libers of about 25 nm diameter made up of 13 protofilaments, each of which consists of a chain of heterodimers of α-and β-tubulin. Microtubules can be assembled in vitro at 37°C in the presence of GTP which is hydrolyzed during the reaction, and they are disassembled at 4°C. In contrast to most other polymers microtubules show the behavior of “dynamic instability”, i.e. they can switch between phases of growth and phases of shrinkage, even at an overall steady state [1]. In certain conditions an entire solution can be synchronized, leading to autonomous oscillations in the degree of assembly which can be observed by X-ray scattering (Fig. 1), light scattering, or electron microscopy [2-5]. In addition such solutions are capable of generating spontaneous spatial patterns [6].In an earlier study we have analyzed the structure of microtubules and their cold-induced disassembly by cryo-EM [7]. One result was that disassembly takes place by loss of protofilament fragments (tubulin oligomers) which fray apart at the microtubule ends. We also looked at microtubule oscillations by time-resolved X-ray scattering and proposed a reaction scheme [4] which involves a cyclic interconversion of tubulin, microtubules, and oligomers (Fig. 2). The present study was undertaken to answer two questions: (a) What is the nature of the oscillations as seen by time-resolved cryo-EM? (b) Do microtubules disassemble by fraying protofilament fragments during oscillations at 37°C?

Do Event-Related Brain Potentials Reflect Mental (Cognitive) Operations?

2002 ◽  
Vol 16 (3) ◽  
pp. 129-149 ◽  
Author(s):  
Boris Kotchoubey
Keyword(s):  
Cognitive Processes ◽  
Point Of View ◽  
Internal Variables ◽  
Brain Potentials ◽  
Cognitive Operations ◽  
External Variables ◽  
Series Of Experiments ◽  
Mental Operations ◽  
A Chain ◽  
Processing Mechanisms

Abstract Most cognitive psychophysiological studies assume (1) that there is a chain of (partially overlapping) cognitive processes (processing stages, mechanisms, operators) leading from stimulus to response, and (2) that components of event-related brain potentials (ERPs) may be regarded as manifestations of these processing stages. What is usually discussed is which particular processing mechanisms are related to some particular component, but not whether such a relationship exists at all. Alternatively, from the point of view of noncognitive (e. g., “naturalistic”) theories of perception ERP components might be conceived of as correlates of extraction of the information from the experimental environment. In a series of experiments, the author attempted to separate these two accounts, i. e., internal variables like mental operations or cognitive parameters versus external variables like information content of stimulation. Whenever this separation could be performed, the latter factor proved to significantly affect ERP amplitudes, whereas the former did not. These data indicate that ERPs cannot be unequivocally linked to processing mechanisms postulated by cognitive models of perception. Therefore, they cannot be regarded as support for these models.

Right-Hemisphere Specialization for Contour Grouping

2014 ◽  
Vol 61 (5) ◽  
pp. 331-339 ◽  
Author(s):  
Gregor Volberg
Keyword(s):  
Right Hemisphere ◽  
Contour Detection ◽  
Global Processing ◽  
Detection Accuracy ◽  
Frequency Spectra ◽  
Visual Hemifield ◽  
Spatial Frequencies ◽  
A Chain ◽  
The Right ◽  
Hemisphere Specialization

Previous studies often revealed a right-hemisphere specialization for processing the global level of compound visual stimuli. Here we explore whether a similar specialization exists for the detection of intersected contours defined by a chain of local elements. Subjects were presented with arrays of randomly oriented Gabor patches that could contain a global path of collinearly arranged elements in the left or in the right visual hemifield. As expected, the detection accuracy was higher for contours presented to the left visual field/right hemisphere. This difference was absent in two control conditions where the smoothness of the contour was decreased. The results demonstrate that the contour detection, often considered to be driven by lateral coactivation in primary visual cortex, relies on higher-level visual representations that differ between the hemispheres. Furthermore, because contour and non-contour stimuli had the same spatial frequency spectra, the results challenge the view that the right-hemisphere advantage in global processing depends on a specialization for processing low spatial frequencies.

A chain model for chromosomes

1961 ◽  
Vol 58 ◽  
pp. 1072-1077 ◽  
Author(s):  
Frank Stahl
Keyword(s):  
Chain Model ◽  
A Chain

Fibrinogen Montreal

1973 ◽  
Vol 29 (03) ◽  
pp. 536-546 ◽  
Author(s):  
M Lacombe ◽  
J Soria ◽  
C Soria ◽  
G d’Angelo ◽  
R Lavallee ◽  
...  
Keyword(s):  
Optical Density ◽  
Polyacrylamide Gel ◽  
Clotting Time ◽  
Functional Defect ◽  
A Chain ◽  
Fibrin Monomers

SummaryA new case of congenital dysfibrinogenemia characterized by a prolonged thrombin clotting time and a low optical density of the polymerization curve has been discovered in Montreal. The functional defect is due to an abnormal aggregation of fibrin monomers.The characteristics of this abnormal fibrinogen are serum gélification (Paracoagulation) at 37°, 22° and 4° C, a normal immuno-electrophoretic and electrofocusing pattern, a slight increase in the mobility in the α (A) chain by electrophoresis of the dissociated chains in polyacrylamide gel. However, no abnormality was found in the α (A) chain of the disulphide knot.

Observations on a Relationship between Steroid Metabolism and the Concentration of Plasma Fibrinogen

1963 ◽  
Vol 10 (02) ◽  
pp. 400-405 ◽  
Author(s):  
B. A Amundson ◽  
L. O Pilgeram
Keyword(s):  
Blood Coagulation ◽  
Methyl Ether ◽  
Broad Spectrum ◽  
Human Subjects ◽  
Plasma Fibrinogen ◽  
Steroid Metabolism ◽  
Specific Site ◽  
Chain Reaction ◽  
Normal Human ◽  
A Chain

SummaryEnovid (5 mg norethynodrel and 0.075 mg ethynylestradiol-3-methyl ether) therapy in young normal human subjects causes an increase in plasma fibrinogen of 32.4% (P >C 0.001). Consideration of this effect together with other effects of Enovid on the activity of specific blood coagulatory factors suggests that the steroids are exerting their effect at a specific site of the blood coagulation and/or fibrinolytic system. The broad spectrum of changes which are induced by the steroids may be attributed to a combination of a chain reaction and feed-back control.

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