scholarly journals Revealing Pre-analytical Pitfalls in Concentration Determination of Peptides by Quantification of Amino Acid Fluorescence

2019 ◽  
Vol 73 (4) ◽  
pp. 330-330
Author(s):  
Martina D. Allenspach ◽  
Jens A. Fuchs ◽  
Christian Steuer
Author(s):  
M. Haider ◽  
B. Bohrmann

The technique of Z-contrast in STEM offers the possibility to determine the local concentration of macromolecules like lipids, proteins or DNA. Contrast formation depends on the atomic composition of the particular structure. In the case of DNA, its phosphorous content discriminates it from other biological macromolecules. In our studies, sections of E. coli, the dinoflagellate Amphidinium carterae and Euglena spec. cells were used which were obtained by cryofixation followed by freeze-substitution into acetone with 3% glutaraldehyde. The samples were then embedded either in Lowicryl HM20 at low temperature or in Epon at high temperature. Sections were coated on both sides with 30Å carbon.The DF- and the inelastic image have been recorded simultaneously with a Cryo-STEM. This Cryo-STEM is equipped with a highly dispersive Electron Energy Loss Spectrometer. With this instrument pure Z-contrast can be achieved either with a Filtered DF-image divided by the inelastic image or, as is used in this paper, by dividing the conventional DF-image by an inelastic image which has been recorded with an inelastic detector whose response is dependent on the total energy loss of the inelastically scattered electrons.


2020 ◽  
Author(s):  
Michele Larocca

<p>Protein folding is strictly related to the determination of the backbone dihedral angles and depends on the information contained in the amino acid sequence as well as on the hydrophobic effect. To date, the type of information embedded in the amino acid sequence has not yet been revealed. The present study deals with these problematics and aims to furnish a possible explanation of the information contained in the amino acid sequence, showing and reporting rules to calculate the backbone dihedral angles φ. The study is based on the development of mechanical forces once specific chemical interactions are established among the side chain of the residues in a polypeptide chain. It aims to furnish a theoretical approach to predict backbone dihedral angles which, in the future, may be applied to computational developments focused on the prediction of polypeptide structures.</p>


1960 ◽  
Vol 235 (1) ◽  
pp. 124-127
Author(s):  
Virginia E. Davis ◽  
J. Awapara
Keyword(s):  

1973 ◽  
Vol 28 (9-10) ◽  
pp. 533-554 ◽  
Author(s):  
Lothar Rafflenbeul ◽  
Wa-Ming Pang ◽  
Hansjürgen Schönert ◽  
Klaus Haberle

Abstract Isopiestic vapor pressure measurements and calorimetric determination of the heat of dilution have been performed and evaluated with respect to enthalpy, entropy and free enthalpy in the ternary solutions water+ glycin+ urea and water+ alanin + urea. The free enthalpy of transfer for the process: Amino acid from water to water+ urea, which can be derived from these measurements, does not agree with the value calculated from solubility measurements. The reason for this discrepancy and the values of entropy and enthalpy in terms of hydrophobic interaction are discussed. Supplementary measurements of the proton magnetic resonance in these solutions are included.


Amino Acids ◽  
2021 ◽  
Author(s):  
Grażyna Gałęzowska ◽  
Joanna Ratajczyk ◽  
Lidia Wolska

AbstractThe quantitation and qualification of amino acids are most commonly used in clinical and epidemiological studies, and provide an excellent way of monitoring compounds in human fluids which have not been monitored previously, to prevent some diseases. Because of this, it is not surprising that scientific interest in evaluating these compounds has resurfaced in recent years and has precipitated the development of a multitude of new analytical techniques. This review considers recent developments in HPLC analytics on the basis of publications from the last few years. It helps to update and systematize knowledge in this area. Particular attention is paid to the progress of analytical methods, pointing out the advantages and drawbacks of the various techniques used for the preparation, separation and determination of amino acids. Depending on the type of sample, the preparation conditions for HPLC analysis change. For this reason, the review has focused on three types of samples, namely urine, blood and cerebrospinal fluid. Despite time-consuming sample preparation before HPLC analysis, an additional derivatization technique should be used, depending on the detection technique used. There are proposals for columns that are specially modified for amino acid separation without derivatization, but the limit of detection of the substance is less beneficial. In view of the fact that amino acid analyses have been performed for years and new solutions may generate increased costs, it may turn out that older proposals are much more advantageous.


1973 ◽  
Vol 248 (7) ◽  
pp. 2387-2391 ◽  
Author(s):  
Gladys E. Deibler ◽  
Russell E. Martenson

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