Molecular Mechanisms Involved in Thermally Induced Gel Formation of Japanese Codling Meat Paste during a Two-Step Heating Procedure

2022 ◽  
Author(s):  
Misaki Uemura ◽  
Takuto Yamamura ◽  
Nanami Mizusawa ◽  
Hiroki Koyama ◽  
Ko Yasumoto ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Gel Formation ◽  
Thermally Induced ◽  
Step Heating

scholarly journals Temperature-dependent local conformations and conformational distributions of cyanine dimer labeled single-stranded -- double-stranded DNA junctions by 2D fluorescence spectroscopy

2021 ◽  
Author(s):  
Dylan Heussman ◽  
Justin Kittell ◽  
Peter H. von Hippel ◽  
Andrew H. Marcus
Keyword(s):  
Fluorescence Spectroscopy ◽  
Molecular Mechanisms ◽  
Protein Complexes ◽  
Structural Disorder ◽  
Spectroscopic Studies ◽  
Sugar Phosphate ◽  
Thermally Induced ◽  
Dna Junctions ◽  
Dna Strands ◽  
Local Conformations

DNA replication, and the related processes of genome expression, require binding, assembly, and function of protein complexes at and near single-stranded (ss) -- double-stranded (ds) DNA junctions. These central protein-DNA interactions are likely influenced by thermally induced conformational fluctuations of the DNA scaffold across an unknown distribution of functionally relevant states to provide regulatory proteins access to properly conformed DNA binding sites. Thus, characterizing the nature of conformational fluctuations and the associated structural disorder at ss-dsDNA junctions is likely critical for understanding the molecular mechanisms of these central biological processes. Here we describe spectroscopic studies of model ss-dsDNA fork constructs that contain dimers of "internally labeled" cyanine (iCy3) chromophore probes that have been rigidly inserted within the sugar-phosphate backbones of the DNA strands. Our combined analyses of absorbance, circular dichroism (CD) and two-dimensional fluorescence spectroscopy (2DFS) permit us to characterize the local conformational parameters and conformational distributions. We find that the DNA sugar-phosphate backbones undergo abrupt successive changes in their local conformations -- initially from a right-handed and ordered DNA state to a disordered splayed-open structure and then to a disordered left-handed conformation -- as the dimer probes are moved across the ss-dsDNA junction. Our results suggest that the sugar-phosphate backbones at and near ss-dsDNA junctions adopt specific position-dependent local conformations and exhibit varying extents of conformational disorder that deviate widely from the Watson-Crick structure. We suggest that some of these conformations are likely to function as secondary-structure motifs for interaction with protein complexes that bind to and assemble at these sites.

scholarly journals Temperature-Dependent Nanomechanics and Topography of Bacteriophage T7

2018 ◽  
Vol 92 (20) ◽  
Author(s):  
Zsuzsanna Vörös ◽  
Gabriella Csík ◽  
Levente Herényi ◽  
Miklós Kellermayer
Keyword(s):  
Heat Treatment ◽  
Structural Changes ◽  
Molecular Mechanisms ◽  
Mechanical Stability ◽  
Structural Constraints ◽  
Thermally Induced ◽  
Force Microscopy ◽  
Partial Denaturation ◽  
Induced Changes ◽  
T7 Phage

ABSTRACT Viruses are nanoscale infectious agents which may be inactivated by heat treatment. The global molecular mechanisms of virus inactivation and the thermally induced structural changes in viruses are not fully understood. In this study, we measured the heat-induced changes in the properties of T7 bacteriophage particles exposed to a two-stage (65°C and 80°C) thermal effect, by using atomic force microscopy (AFM)-based nanomechanical and topographical measurements. We found that exposure to 65°C led to the release of genomic DNA and to the loss of the capsid tail; hence, the T7 particles became destabilized. Further heating to 80°C surprisingly led to an increase in mechanical stability, due likely to partial denaturation of the capsomeric proteins kept within the global capsid arrangement. IMPORTANCE Even though the loss of DNA, caused by heat treatment, destabilizes the T7 phage, its capsid is remarkably able to withstand high temperatures with a more or less intact global topographical structure. Thus, partial denaturation within the global structural constraints of the viral capsid may have a stabilizing effect. Understanding the structural design of viruses may help in constructing artificial nanocapsules for the packaging and delivery of materials under harsh environmental conditions.

Morphologies of Nonadherent Al2O3 and Matching Substrate Surfaces

1972 ◽  
Vol 30 ◽  
pp. 524-525
Author(s):  
C. S. Giggins ◽  
J. K. Tien ◽  
B. H. Kear ◽  
F. S. Pettit
Keyword(s):  
Electron Microscopy ◽  
Oxide Scale ◽  
Oxidation Resistance ◽  
Substrate Surface ◽  
Morphological Features ◽  
Thermally Induced ◽  
Oxide Spallation ◽  
Oxidation Resistant ◽  
Induced Stresses ◽  
Substrate Surfaces

The performance of most oxidation resistant alloys and coatings is markedly improved if the oxide scale strongly adheres to the substrate surface. Consequently, in order to develop alloys and coatings with improved oxidation resistance, it has become necessary to determine the conditions that lead to spallation of oxides from the surfaces of alloys. In what follows, the morphological features of nonadherent Al2O3, and the substrate surfaces from which the Al2O3 has spalled, are presented and related to oxide spallation.The Al2O3, scales were developed by oxidizing Fe-25Cr-4Al (w/o) and Ni-rich Ni3 (Al,Ta) alloys in air at 1200°C. These scales spalled from their substrates upon cooling as a result of thermally induced stresses. The scales and the alloy substrate surfaces were then examined by scanning and replication electron microscopy.The Al2O3, scales from the Fe-Cr-Al contained filamentary protrusions at the oxide-gas interface, Fig. 1(a). In addition, nodules of oxide have been developed such that cavities were formed between the oxide and the substrate, Fig. 1(a).

Transcription factor/DNA interactions visualized by electron spectroscopic imaging

1992 ◽  
Vol 50 (1) ◽  
pp. 450-451
Author(s):  
David P. Bazett-Jones ◽  
Mark L. Brown
Keyword(s):  
Transcription Factor ◽  
Dna Sequences ◽  
Transcription Initiation ◽  
Molecular Mechanisms ◽  
Phosphorus Content ◽  
Spectroscopic Imaging ◽  
Electron Spectroscopic Imaging ◽  
Dna Backbone ◽  
Two Parameters ◽  
High Level

A multisubunit RNA polymerase enzyme is ultimately responsible for transcription initiation and elongation of RNA, but recognition of the proper start site by the enzyme is regulated by general, temporal and gene-specific trans-factors interacting at promoter and enhancer DNA sequences. To understand the molecular mechanisms which precisely regulate the transcription initiation event, it is crucial to elucidate the structure of the transcription factor/DNA complexes involved. Electron spectroscopic imaging (ESI) provides the opportunity to visualize individual DNA molecules. Enhancement of DNA contrast with ESI is accomplished by imaging with electrons that have interacted with inner shell electrons of phosphorus in the DNA backbone. Phosphorus detection at this intermediately high level of resolution (≈lnm) permits selective imaging of the DNA, to determine whether the protein factors compact, bend or wrap the DNA. Simultaneously, mass analysis and phosphorus content can be measured quantitatively, using adjacent DNA or tobacco mosaic virus (TMV) as mass and phosphorus standards. These two parameters provide stoichiometric information relating the ratios of protein:DNA content.

Dissection of the molecular mechanisms of protein targeting to the peroxisome using immunofluorescence and immunocryoelectron microscopies

1990 ◽  
Vol 48 (3) ◽  
pp. 44-45
Author(s):  
G-A. Keller ◽  
S. J. Gould ◽  
S. Subramani ◽  
S. Krisans
Keyword(s):  
Mammalian Cells ◽  
Molecular Mechanisms ◽  
Protein Targeting ◽  
Firefly Luciferase ◽  
Peroxisomal Enzyme ◽  
Transfected Cells ◽  
Peroxisomal Targeting ◽  
Targeting Signal ◽  
Series Of Experiments ◽  
Peroxisomal Targeting Signal

Subcellular compartments within eukaryotic cells must each be supplied with unique sets of proteins that must be directed to, and translocated across one or more membranes of the target organelles. This transport is mediated by cis- acting targeting signals present within the imported proteins. The following is a chronological account of a series of experiments designed and carried out in an effort to understand how proteins are targeted to the peroxisomal compartment.-We demonstrated by immunocryoelectron microscopy that the enzyme luciferase is a peroxisomal enzyme in the firefly lantern. -We expressed the cDNA encoding firefly luciferase in mammalian cells and demonstrated by immunofluorescence that the enzyme was transported into the peroxisomes of the transfected cells. -Using deletions, linker insertions, and gene fusion to identify regions of luciferase involved in its transport to the peroxisomes, we demonstrated that luciferase contains a peroxisomal targeting signal (PTS) within its COOH-terminal twelve amino acid.

Applications of ultramicrotomy for materials characterization

1993 ◽  
Vol 51 ◽  
pp. 232-233
Author(s):  
R.T. Blackham ◽  
J.J. Haugh ◽  
C.W. Hughes ◽  
M.G. Burke
Keyword(s):  
Materials Science ◽  
Microstructural Analysis ◽  
Analytical Electron Microscopy ◽  
Austenitic Stainless Steels ◽  
Specimen Preparation ◽  
Preparation Technique ◽  
Thermally Induced ◽  
Radiation Induced ◽  
Characterization Of Materials

Essential to the characterization of materials using analytical electron microscopy (AEM) techniques is the specimen itself. Without suitable samples, detailed microstructural analysis is not possible. Ultramicrotomy, or diamond knife sectioning, is a well-known mechanical specimen preparation technique which has been gaining attention in the materials science area. Malis and co-workers and Glanvill have demonstrated the usefulness and applicability of this technique to the study of a wide variety of materials including Al alloys, composites, and semiconductors. Ultramicrotomed specimens have uniform thickness with relatively large electron-transparent areas which are suitable for AEM anaysis.Interface Analysis in Type 316 Austenitic Stainless Steel: STEM-EDS microanalysis of grain boundaries in austenitic stainless steels provides important information concerning the development of Cr-depleted zones which accompany M23C6 precipitation, and documentation of radiation induced segregation (RIS). Conventional methods of TEM sample preparation are suitable for the evaluation of thermally induced segregation, but neutron irradiated samples present a variety of problems in both the preparation and in the AEM analysis, in addition to the handling hazard.

High resolution mapping of nucleic acid containing complexes in vitro and in situ

1996 ◽  
Vol 54 ◽  
pp. 48-49
Author(s):  
D. P. Bazett-Jones ◽  
M. J. Hendzel
Keyword(s):  
Nucleic Acid ◽  
High Resolution ◽  
Transcription Initiation ◽  
Molecular Mechanisms ◽  
Heavy Atom ◽  
Regulation Of Transcription ◽  
High Exposure ◽  
Resolution Mapping ◽  
Tata Sequence

Structural analysis of combinations of nucleosomes and transcription factors on promoter and enhancer elements is necessary in order to understand the molecular mechanisms responsible for the regulation of transcription initiation. Such complexes are often not amenable to study by high resolution crystallographic techniques. We have been applying electron spectroscopic imaging (ESI) to specific problems in molecular biology related to transcription regulation. There are several advantages that this technique offers in studies of nucleoprotein complexes. First, an intermediate level of spatial resolution can be achieved because heavy atom contrast agents are not necessary. Second, mass and stoichiometric relationships of protein and nucleic acid can be estimated by phosphorus detection, an element in much higher proportions in nucleic acid than protein. Third, wrapping or bending of the DNA by the protein constituents can be observed by phosphorus mapping of the complexes. Even when ESI is used with high exposure of electrons to the specimen, important macromolecular information may be provided. For example, an image of the TATA binding protein (TBP) bound to DNA is shown in the Figure (top panel). It can be seen that the protein distorts the DNA away from itself and much of its mass sits off the DNA helix axis. Moreover, phosphorus and mass estimates demonstrate whether one or two TBP molecules interact with this particular promoter TATA sequence.

Spin-crossover in an iron(iii) complex showing a broad thermal hysteresis

2021 ◽  
Author(s):  
Cyril Rajnák ◽  
Romana Mičová ◽  
Ján Moncoľ ◽  
Ľubor Dlháň ◽  
Christoph Krüger ◽  
...  
Keyword(s):  
Schiff Base ◽  
Schiff Base Ligand ◽  
Spin Crossover ◽  
Thermal Hysteresis ◽  
Mononuclear Complex ◽  
Hysteresis Width ◽  
Thermally Induced

A pentadentate Schiff-base ligand 3,5Cl-L2− and NCSe− form a iron(iii) mononuclear complex [Fe(3,5Cl-L)(NCSe)], which shows a thermally induced spin crossover with a broad hysteresis width of 24 K between 123 K (warming) and 99 K (cooling).

How do histone modifications contribute to transgenerational epigenetic inheritance in C. elegans?

2020 ◽  
Vol 48 (3) ◽  
pp. 1019-1034 ◽  
Author(s):  
Rachel M. Woodhouse ◽  
Alyson Ashe
Keyword(s):  
Histone Modifications ◽  
Molecular Mechanisms ◽  
Epigenetic Inheritance ◽  
Nematode Caenorhabditis Elegans ◽  
Histone Methyltransferases ◽  
Transgenerational Epigenetic Inheritance ◽  
C Elegans ◽  
Recent Developments ◽  
Gene Regulatory

Gene regulatory information can be inherited between generations in a phenomenon termed transgenerational epigenetic inheritance (TEI). While examples of TEI in many animals accumulate, the nematode Caenorhabditis elegans has proven particularly useful in investigating the underlying molecular mechanisms of this phenomenon. In C. elegans and other animals, the modification of histone proteins has emerged as a potential carrier and effector of transgenerational epigenetic information. In this review, we explore the contribution of histone modifications to TEI in C. elegans. We describe the role of repressive histone marks, histone methyltransferases, and associated chromatin factors in heritable gene silencing, and discuss recent developments and unanswered questions in how these factors integrate with other known TEI mechanisms. We also review the transgenerational effects of the manipulation of histone modifications on germline health and longevity.

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