scholarly journals Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal

Biopolymers ◽  
2011 ◽  
Vol 97 (4) ◽  
pp. 240-249 ◽  
Author(s):  
Joanna Makowska ◽  
Adam Liwo ◽  
Wioletta Żmudzińska ◽  
Agnieszka Lewandowska ◽  
Lech Chmurzyński ◽  
...  
Keyword(s):  
Charged Residues ◽  
Chain Reversal ◽  
A Chain

The Determination of “Head-Head” and “Tail-Tail” Structures in Poly(Isoprene)S

1972 ◽  
Vol 45 (5) ◽  
pp. 1295-1302 ◽  
Author(s):  
Marjorie J. Hackathorn ◽  
M. J. Brock
Keyword(s):  
Gas Chromatography ◽  
Free Radical ◽  
Natural Rubber ◽  
Pyrolysis Gas ◽  
Pyrolysis Gas Chromatography ◽  
Chain Reversal ◽  
A Chain

Abstract Pyrolysis-gas chromatography has indicated the presence of head-head structures in free radical initiated poly(isoprene)s. Microozonolysis has confirmed the presence of both head-head (15-20 per cent) and tail-tail (4-7 per cent) structures in these polymers. These structures (which are absent in natural rubber) are present in lesser amounts in Lithium and Ziegler poly(isoprene)s (1-3 per cent). Non-equivalent amounts of head-head and tail-tail structures in particular samples indicate a chain reversal in which neither head nor tail units are involved. It has been postulated that chain reversal may occur at points of 3,4 addition.

scholarly journals Sequence-specific 1H-n.m.r. assignments and peptide backbone conformation in rat epidermal growth factor

1989 ◽  
Vol 257 (1) ◽  
pp. 197-205 ◽  
Author(s):  
K H Mayo ◽  
R C Cavalli ◽  
A R Peters ◽  
R Boelens ◽  
R Kaptein
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Resonance Assignments ◽  
Structural Features ◽  
Terminal Segment ◽  
Beta Sheet ◽  
Peptide Backbone ◽  
Epidermal Growth ◽  
Chain Reversal ◽  
A Chain

The solution conformation of rat epidermal growth factor (EGF) has been investigated by proton n.m.r. techniques. Two-dimensional proton n.m.r. experiments have allowed sequential resonance assignments to be made for most protons. On the basis of these assignments, two regions of anti-parallel beta-sheet structure have been derived from the n.m.r. data. A beta-sheet segment running from about V19 to V23 (capital letters refer to amino acids in the single-letter notation) is folded onto a beta-sheet segment running from R28 to N32 and joined by a chain reversal from E24 to D27. A second region involves a beta-turn from V34 to Y37, which starts a short beta-sheet up to G39, followed by a chain reversal up to Q43, which leads to folding of the C-terminal beta-sheet segment, i.e. H44-R45, running antiparallel to the short Y37 beta-sheet segment. The N-terminal segment up to G18 exists in a multiple bend conformation and is folded on to the V29-V23/R28-N32 beta-sheet such that Y10, Y13, Y22 and Y29 are proximal to each other. Structural comparison of rat, murine and human EGFs indicates a number of highly conserved structural features common to at least these species of EGF.

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.

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