1.4 Geometry of bases, sugars, and phosphate groups

2005 ◽  
pp. 18-21
Author(s):  
W. Saenger
Keyword(s):  
Phosphate Groups

Ultrastructural localization of specific nucleoprotein fractions

1978 ◽  
Vol 36 (2) ◽  
pp. 204-205
Author(s):  
G. L. Brown
Keyword(s):  
Gel Electrophoresis ◽  
Mouse Liver ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ultrastructural Localization ◽  
Polyacrylamide Gel ◽  
Acid Extraction ◽  
Acid Solutions ◽  
Low Salt ◽  
Liver Nuclei ◽  
Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

ИЗУЧЕНИЕ СТРУКТУРЫ ДНК В ПЛЕНКАХ МЕТОДОМ ИК-ФУРЬЕ-СПЕКТРОСКОПИИ

2020 ◽  
Vol 65 (6) ◽  
pp. 1058-1064
Author(s):  
С.В. Пастон ◽  
◽  
А.М. Поляничко ◽  
О.В. Шуленина ◽  
Д.Н. Осинникова ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Hydration Shell ◽  
Aqueous Environment ◽  
Ir Absorption ◽  
Sodium Ions ◽  
High Molecular Weight Dna ◽  
Dna Hydration ◽  
Na Ions ◽  
Phosphate Groups ◽  
Dna Film

The aqueous environment and ionic surrounding are the most important factors determining the conformation of DNA and its functioning in the cell. The specificity of the interaction between DNA and cations is especially pronounced with a decrease in water activity. In this work, we studied the B-A transition in high molecular weight DNA with a decrease of humidity in the film with different contents of Na+ ions using FTIR spectroscopy. The IR spectrum of DNA is not only very sensitive to the state of its secondary structure, but also allows us to estimate the amount of water bound to DNA. Upon dehydration of the DNA film, changes characteristic of the B-A transition were observed in the IR absorption spectrum. Using thermogravimetric analysis, it was shown that the degree of DNA hydration reaches the saturation level at a relative humidity of 60% and decreases slightly upon further drying. It has been established that with increasing Na+ concentration, the amount of water strongly bound to DNA decreases. Along with it, sodium ions destroy the hydration shell of DNA and are able to interact directly with phosphate groups.

scholarly journals Phosphorus Kβ X-Ray emission spectroscopy detects non-covalent interactions of phosphate biomolecules in situ

2021 ◽  
Author(s):  
Zachary Mathe ◽  
Olivia McCubbin Stepanic ◽  
Sergey Peredkov ◽  
Serena DeBeer
Keyword(s):  
Nucleic Acids ◽  
Emission Spectroscopy ◽  
Adenine Nucleotides ◽  
X Ray ◽  
Non Covalent Interactions ◽  
Covalent Interactions ◽  
Phosphate Groups

Phosphorus is ubiquitous in biochemistry, found in the phosphate groups of nucleic acids and the energy-transferring system of adenine nucleotides (e.g. ATP). Kβ X-ray emission spectroscopy (XES) at phosphorus has...

The physiology of teichoic acid deficient staphylococci

1973 ◽  
Vol 19 (11) ◽  
pp. 1393-1399 ◽  
Author(s):  
Li-Tse Ou ◽  
A. N. Chatterjee ◽  
F. E. Young ◽  
R. E. Marquis
Keyword(s):  
Cell Walls ◽  
Parent Strain ◽  
Teichoic Acid ◽  
Low Ph ◽  
Aureus Strain ◽  
Binding Affinities ◽  
Inhibitory Effects ◽  
Growth Inhibitory ◽  
Acid Titration ◽  
Phosphate Groups

Cell walls isolated from a teichoic acid deficient mutant (52A5) of Staphylococcus aureus strain H were found to have lower capacities to bind cations than did walls of the parent strain. Both types of walls had higher binding affinities for Mg2+ and Ca2+ than for K+ and Na+. The reduced number of phosphate groups in 52A5 walls was reflected in a higher apparent pKa of 4.3 for displacement of Mg2+ (or Ca2+) during acid titration with HCl. The comparable pKa value for displacement of bound Mg2+ from parent-strain walls was 3.7. The reduced capacity of 52A5 walls to bind cations was not reflected in any significant increase in sensitivity to the growth inhibitory actions of ethylenediaminetetraacetate, low pH, or high NaCl concentrations. However, the 52A5 strain was somewhat more sensitive to the inhibitory effects of high pH. Also, mutant walls were found to be structurally more compact than walls of the parent strain, presumably because of less extensive electrostatic repulsion within the wall matrix.

The infra-red spectrum and molecular configuration of sodium deoxyribonucleate

1957 ◽  
Vol 239 (1219) ◽  
pp. 446-463 ◽  
Keyword(s):  
Relative Humidity ◽  
Vapour Phase ◽  
Molecular Configuration ◽  
Absorption Bands ◽  
Oriented Films ◽  
Infra Red ◽  
Modes Of Vibration ◽  
Water Measurement ◽  
Phosphate Groups ◽  
Polarized Radiation

The infra-red spectra of oriented films of sodium deoxyribonucleate have been investigated between 700 and 4000 cm -1 using polarized radiation and under varying degrees of relative humidity. Similar spectra have been obtained when the films have been deuterated by vapour-phase exchange with heavy water. It is found that the infra-red dichroism of nearly every band increases with the relative humidity. Many of the principal absorption bands can be assigned to separable modes of vibration in the bases, the phosphate groups or the absorbed water. Measurement of the dichroic ratios of certain of these bands indicates that at high relative humidity the bases must be nearly perpendicular to the orientation direction. The configuration deduced for the phosphate groups is unlike that proposed in the Crick-Watson model, but is in essential agreement with that recently proposed by Wilkins and his co-workers. Some observations are also reported on the corresponding spectra of sodium ribonucleate. Since no dichroism was observed, no conclusions can be drawn regarding the molecular configuration of this polymer.

scholarly journals The Terminal Phosphate Groups of Tobacco Mosaic Virus

1960 ◽  
Vol 235 (4) ◽  
pp. 1014-1018 ◽  
Author(s):  
M.P. Gordon ◽  
B. Singer ◽  
H. Fraenkel-Conrat
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Phosphate Groups

scholarly journals Determination of the steady-state turnover rates of the metabolically active pools of phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate in human erythrocytes

1989 ◽  
Vol 259 (3) ◽  
pp. 893-896 ◽  
Author(s):  
C E King ◽  
P T Hawkins ◽  
L R Stephens ◽  
R H Michell
Keyword(s):  
Steady State ◽  
Rate Constants ◽  
Human Erythrocytes ◽  
Turnover Rates ◽  
Metabolic Fluxes ◽  
Metabolic Pool ◽  
Phosphatidylinositol 4 ◽  
Kinetics Of ◽  
Phosphate Groups

When intact human erythrocytes are incubated at metabolic steady state in a chloride-free medium containing [32P]Pi, there is rapid labelling of the gamma-phosphate of ATP, followed by a slower labelling of the monoester phosphate groups of phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] [King, Stephens, Hawkins, Guy & Michell (1987) Biochem. J. 244, 209-217]. We have analysed the early kinetics of the labelling of these phosphate groups, in order to determine: (a) the steady-state rates of the interconversions of phosphatidylinositol, PtdIns4P and PtdIns(4,5)P2; and (b) the fractions of the total cellular complement of PtdIns4P and PtdIns(4,5)P2 that participate in this steady-state turnover. The experimental data most closely fit a pattern of PtdIns4P and PtdIns(4,5)P2 turnover in which one-quarter of the total cellular complement of each lipid is in the metabolic pool that participates in rapid metabolic turnover, with rate constants of 0.028 min-1 for the interconversion of PtdIns and PtdIns4P, and of 0.010 min-1 for the PtdIns4P/PtdIns(4,5)P2 cycle. These rate constants represent metabolic fluxes of approx. 2.1 nmol of lipid/h per ml of packed erythrocytes between PtdIns and PtdIns4P and of approx. 5.7 nmol/h per ml of cells between PtdIns4P and PtdIns(4,5)P2.

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