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Volume 35, Issue 1
Displaying 1-12 of 12 articles from this issue
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Katsuhide YUTANI1995 Volume 35 Issue 1 Pages 3-7
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSThermodynamics of protein denaturation has been investigated by calorimetry. Analyzing the excess heat capacity curve of a protein obtained using an adiabatic differential scanning calorimeter, we can get important thermodynamic parameters of protein denaturation such as heat capacity change of denaturation and temperature functions of denaturation enthalpy, denaturation entropy, and denaturation Gibbs energy. In this paper, the thermodynamic parameters have been discussed to elucidate the role of each amino acid residue in conformational stability of a protein.View full abstractDownload PDF (337K) -
Yoshimi MAEDA1995 Volume 35 Issue 1 Pages 8-11
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSThe effect of anions and cations on the stepwise melting of plasmid DNA was studied by means of differential scanning calorimetry. The melting profiles of DNA are different depending upon the type of anions; oxoacids and non-oxoacids. With an increase in the concentration of cations, the melting temperature of DNA increases, passes through a maximum, and then decreases.View full abstractDownload PDF (749K) -
Shinichi KITAMURA1995 Volume 35 Issue 1 Pages 12-15
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSMulti-stranded structures, which have been found for certain polysaccharides, are stabilized by cooperation of numerous nonbonded interactions between sugar molecules. Since these cooperative structures undergo conformational transitions with changing temperature, information concerning these structures can be obtained by DSC. As a current example, DSC studies of triple helical polysaccharides, (1→6) branched (1→3)-β-D-glucas are presented.View full abstractDownload PDF (659K) -
Harumi FUKADA1995 Volume 35 Issue 1 Pages 16-19
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSWhile thermodynamic quantities of the specific binding of a protein to another protein is known from isothermal calorimetry, the thermodynamic stabilization introduced by the interaction is also studied by scanning calorimetry. The stabilization is caused by the dissociation process during the unfolding of the comlex. In this article, the two calorimetric methods to determine thermodynamic properties of protein-protein interactions are described.View full abstractDownload PDF (1439K) -
Akinori SARAI1995 Volume 35 Issue 1 Pages 20-24
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSThe recognition of a Specific DNA site by proteins plays a central in the control of gene expression. In order to understand the mechanism of protein-DNA binding and specific sequence recognition, not only structural information but also thermodynamic information on the binding process will be necessary. This article reviews the thermodynamic analyses on the DNA-binding proteins and their interactions with DNA.View full abstractDownload PDF (1360K) -
Akihiro KAGEMOTO1995 Volume 35 Issue 1 Pages 25-28
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSWe have studied on the interaction modes between DNA and cis-platin, adriamycin, and/or fluorouracil, and between DNA and dyes using the calorimeters such as a differential scanning calorimeter and a flow type microcalorimeter.
It has been found that cis-platin bound predominantly to d(GpG) sequence rather than d(ApG) one in DNA and its binding mode was chelation of cis-platin to N7-N7 of two adjacent guanine in DNA, however, adriamycin and/or fluorouracil formed thermodynamically the stable complex with DNA based on an electrostatic interaction, intercalation, and/or hydrogen bond and the binding mode of adriamycin and/or flurouracil for DNA was different in comparison with that for cis-platin.
On the other hand, the thermodynamic studies for dyes intercalated into adjacent base pair of DNA have been carried out by means of heats of mixing and spectrophotometry, and also an analysis for base specificity of dye accompanying the interaction was carried out. From the results, we found that DNA formed thermodynamically the stable complex based on the intercalation of dye into an adjacent base pair and side binding.View full abstractDownload PDF (658K) -
Ichiro HATTA1995 Volume 35 Issue 1 Pages 29-31
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSBased upon the behavior of phase transitions in phospholipid systems, we can consider the interaction between a phospholipid bilayer and molecules, which are, for instance, a small molecule such as cholesterol, an acidic polypeptide such as poly (L-lysine) and a small protein such as melittin. The phase transitions are sensitively influenced by the interactions, where small molecule enters into the bilayer, the acidic polypeptide is adsorbed on the surface of the bilayer, and the small protein goes through the bilayer. By making efficient use of calorimetric measurements, we can discuss the way of the interaction in these typical cases from the viewpoint of thermodynamical stability.View full abstractDownload PDF (176K) -
Katsutada TAKAHASHI1995 Volume 35 Issue 1 Pages 32-35
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSA method to determine calorimetrically the growth activity of living microbial cells is outlined. A multiplex calorimeter was constructed to detect quantitatively the metabolic heat evolved during microbial growth and applied to characterize the growth behaviors of microbes under various conditions. The effect of various drugs on microbial growth activities was studied and the drug potency curves drawn on the basis of their results were shown.View full abstractDownload PDF (1199K) -
Yuji MIYAZAKI1995 Volume 35 Issue 1 Pages 36-39
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSThe low-temperature behavior of tetragonal lysozyme and monoclinic myoglobin crystals was investigated with an adiabatic microcalorimeter. Glass transitions were obseived in both crystals. From the water content dependence of the glass transition temperatures, it is concluded that the glass transitions are due to the immobilization of the cooperative motions among the protein molecules and the crystal water molecules.View full abstractDownload PDF (673K) -
Atsuo TAMURA1995 Volume 35 Issue 1 Pages 40-43
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSIt has been known that proteins can be denatured not only by increasing the temperature but also by decreasing it. The latter phenomenon, which is normally called "cold denaturation", shows common features of protein unfolding as well as characteristics that are specific to each protein.View full abstractDownload PDF (734K) -
[in Japanese]1995 Volume 35 Issue 1 Pages 44-46
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSDownload PDF (244K) -
1995 Volume 35 Issue 1 Pages 47-49
Published: January 25, 1995
Released on J-STAGE: July 09, 2009
JOURNAL FREE ACCESSDownload PDF (1435K)
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