scholarly journals A spectrophotometric study of the secondary structure of ribonucleic acid based on a method for diminishing single-stranded base-‘stacking’ without affecting multi-helical structures

1967 ◽  
Vol 103 (3) ◽  
pp. 749-758 ◽  
Author(s):  
RA Cox ◽  
K Kanagalingam
Keyword(s):  
Secondary Structure ◽  
Ribonucleic Acid ◽  
Spectrophotometric Study ◽  
Base Stacking ◽  
Helical Structures

scholarly journals A spectrophotometric study of the secondary structure of ribonucleic acid isolated from the smaller and larger ribosomal subparticles of rabbit reticulocytes

1970 ◽  
Vol 117 (1) ◽  
pp. 101-118 ◽  
Author(s):  
R. A. Cox
Keyword(s):  
Escherichia Coli ◽  
Ionic Strength ◽  
Secondary Structure ◽  
Ribonucleic Acid ◽  
Spectrophotometric Study ◽  
Urea Concentration ◽  
Model Systems ◽  
Base Pairs ◽  
Virus Like Particles ◽  
Rabbit Reticulocytes

The spectrum of RNA from the smaller and larger subparticles of rabbit reticulocyte ribosomes was studied as a function of pH, ionic strength, urea concentration and temperature. It was inferred that both RNA species form short double-helical segments of not more than about 10 base-pairs in length. Not more than about 70% of the base residues may be located in double-helical segments. RNA from the larger subparticle is richer in guanine and cytosine residues and its secondary structure is the more stable. These conclusions are based on the use of double-helical RNA from virus-like particles and of unfractionated Escherichia coli tRNA as model systems.

scholarly journals A spectrophotometric study of the secondary structure of precursor ribosomal ribonucleic acid from Krebs ascites-tumour cells

1973 ◽  
Vol 135 (2) ◽  
pp. 349-351 ◽  
Author(s):  
A. A. Hadjiolov ◽  
R. A. Cox
Keyword(s):  
Secondary Structure ◽  
Ribonucleic Acid ◽  
18S Rrna ◽  
Spectrophotometric Study ◽  
Spectrophotometric Analysis ◽  
28S Rrna ◽  
Ascites Tumour ◽  
Helical Content ◽  
Ribosomal Ribonucleic Acid ◽  
Ascites Tumour Cells

The spectrophotometric analysis of 45S precursor rRNA shows that it contains more G and C residues than does mature 28S or 18S rRNA. The helical content and the length of double-helical segments in 45S and 28S rRNA are similar.

Secondary Structure of Ribonucleic Acid in Solution

Nature ◽  
1959 ◽  
Vol 184 (4689) ◽  
pp. 818-819 ◽  
Author(s):  
R. A. COX ◽  
U. Z. LITTAUER
Keyword(s):  
Secondary Structure ◽  
Ribonucleic Acid

Studies on the secondary structure of phenylalanyl transfer ribonucleic acid

Biochemistry ◽  
1970 ◽  
Vol 9 (25) ◽  
pp. 4971-4980 ◽  
Author(s):  
Alita Rosenfeld ◽  
Charles L. Stevens ◽  
Morton P. Printz
Keyword(s):  
Secondary Structure ◽  
Ribonucleic Acid

scholarly journals In situFTIR Assessment of Desiccation-Tolerant Tissues

2003 ◽  
Vol 17 (2-3) ◽  
pp. 297-313 ◽  
Author(s):  
Willem F. Wolkers ◽  
Folkert A. Hoekstra
Keyword(s):  
Secondary Structure ◽  
Desiccation Tolerance ◽  
Higher Plants ◽  
Protein Secondary Structure ◽  
Biological Tissues ◽  
Glassy Matrix ◽  
Vibration Band ◽  
Helical Structures ◽  
Ftir Studies ◽  
Stretching Vibration

This essay shows how Fourier transform infrared (FTIR) microspectroscopy can be applied to study thermodynamic parameters and conformation of endogenous biomolecules in desiccation-tolerant biological tissues. Desiccation tolerance is the remarkable ability of some organisms to survive complete dehydration. Seed and pollen of higher plants are well known examples of desiccation-tolerant tissues. FTIR studies on the overall protein secondary structure indicate that during the acquisition of desiccation tolerance, plant embryos exhibit proportional increases inα-helical structures and thatµ-sheet structures dominate upon drying of desiccation sensitive-embryos. During ageing of pollen and seeds, the overall protein secondary structure remains stable, whereas drastic changes in the thermotropic response of membranes occur, which coincide with a complete loss of viability. Properties of the cytoplasmic glassy matrix in desiccation-tolerant plant organs can be studied by monitoring the position of the OH-stretching vibration band of endogenous carbohydrates and proteins as a function of temperature. By applying these FTIR techniques to maturation-defective mutant seeds ofArabidopsis thalianawe were able to establish a correlation between macromolecular stability and desiccation tolerance. Taken together,in situFTIR studies can give unique information on conformation and stability of endogenous biomolecules in desiccation-tolerant tissues.

scholarly journals Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics

Molecules ◽  
2021 ◽  
Vol 26 (24) ◽  
pp. 7650
Author(s):  
Tatijana Markoska ◽  
Davor Daniloski ◽  
Todor Vasiljevic ◽  
Thom Huppertz
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Fourier Transform ◽  
Magnetic Resonance ◽  
Secondary Structure ◽  
Structural Changes ◽  
Hydrophobic Interactions ◽  
Fourier Transform Infrared ◽  
Helical Structures ◽  
Random Coils ◽  
Α Helix

This study investigated structural changes in β-casein as a function of temperature (4 and 20 °C) and pH (5.9 and 7.0). For this purpose, nuclear magnetic resonance (NMR) and Fourier-transform infrared (FTIR) spectroscopy were used, in conjunction with chemometric analysis. Both temperature and pH had strongly affected the secondary structure of β-casein, with most affected regions involving random coils and α-helical structures. The α-helical structures showed great pH sensitivity by decreasing at 20 °C and diminishing completely at 4 °C when pH was increased from 5.9 to 7.0. The decrease in α-helix was likely related to the greater presence of random coils at pH 7.0, which was not observed at pH 5.9 at either temperature. The changes in secondary structure components were linked to decreased hydrophobic interactions at lower temperature and increasing pH. The most prominent change of the α-helix took place when the pH was adjusted to 7.0 and the temperature set at 4 °C, which confirms the disruption of the hydrogen bonds and weakening of hydrophobic interactions in the system. The findings can assist in establishing the structural behaviour of the β-casein under conditions that apply as important for solubility and production of β-casein.

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