scholarly journals THE DETERMINATION OF PEPTIDE BONDS IN CRYSTALLINE LACTOGLOBULIN

1939 ◽  
Vol 131 (1) ◽  
pp. 387-395
Author(s):  
Rollin D. Hotchkiss
Keyword(s):  
Peptide Bonds

Determination of Total Urinary Protein, Combining Lowry Sensitivity and Biuret Specificity

1973 ◽  
Vol 19 (10) ◽  
pp. 1170-1178 ◽  
Author(s):  
Karl Doetsch ◽  
Richard H Gadsden
Keyword(s):  
Ion Exchange ◽  
Copper Complex ◽  
Biological Fluids ◽  
Gel Filtration ◽  
Urinary Protein ◽  
Peptide Bonds ◽  
Highly Sensitive ◽  
Filtration Step ◽  
Sensitive Method

Abstract A highly sensitive method with specificity for the peptide chain backbone was developed for determination of total urinary protein. Interfering substances are removed by gel filtration and cupric ions are stoichiometrically bound to the peptide bonds of protein by the biuret reaction. Ion-exchange characteristics of the gel are neutralized, allowing protein—copper complex to be separated from excess cupric ions by a second gel filtration step. Copper bound to peptide bonds is colorimetrically determined by use of sodium diethyldithiocarbamate. Nonprotein substances do not interfere unless they simultaneously bind to protein and chelate copper. As little as 1 mg of total protein per deciliter can be determined in heterogeneous biological fluids such as urine.

scholarly journals Large facilities and the evolving ribosome, the cellular machine for genetic-code translation

2009 ◽  
Vol 6 (suppl_5) ◽  
Author(s):  
Ada Yonath
Keyword(s):  
Synchrotron Radiation ◽  
Genetic Code ◽  
Structural Information ◽  
Peptide Bond ◽  
Polymerase Activity ◽  
Resistance Mechanisms ◽  
Peptide Bond Formation ◽  
Peptide Bonds ◽  
Polypeptide Chains

Well-focused X-ray beams, generated by advanced synchrotron radiation facilities, yielded high-resolution diffraction data from crystals of ribosomes, the cellular nano-machines that translate the genetic code into proteins. These structures revealed the decoding mechanism, localized the mRNA path and the positions of the tRNA molecules in the ribosome and illuminated the interactions of the ribosome with initiation, release and recycling factors. They also showed that the ribosome is a ribozyme whose active site is situated within a universal symmetrical region that is embedded in the otherwise asymmetric ribosome structure. As this highly conserved region provides the machinery required for peptide bond formation and for ribosome polymerase activity, it may be the remnant of the proto-ribosome, a dimeric pre-biotic machine that formed peptide bonds and non-coded polypeptide chains. Synchrotron radiation also enabled the determination of structures of complexes of ribosomes with antibiotics targeting them, which revealed the principles allowing for their clinical use, revealed resistance mechanisms and showed the bases for discriminating pathogens from hosts, hence providing valuable structural information for antibiotics improvement.

Partial Vapor-Phase Hydrolysis of Peptide Bonds: A Method for Mass Spectrometric Determination of O-Glycosylated Sites in Glycopeptides

1999 ◽  
Vol 269 (1) ◽  
pp. 54-65 ◽  
Author(s):  
Ekaterina Mirgorodskaya ◽  
Helle Hassan ◽  
Hans H. Wandall ◽  
Henrik Clausen ◽  
Peter Roepstorff
Keyword(s):  
Vapor Phase ◽  
Mass Spectrometric ◽  
Peptide Bonds ◽  
Mass Spectrometric Determination ◽  
Hydrolysis Of ◽  
Vapor Phase Hydrolysis

Effect of Non-Peptide and Non-Protein Nitrogen Compounds for the Determination of Protein Content by near Infrared Spectroscopy

1994 ◽  
Vol 2 (3) ◽  
pp. 145-151 ◽  
Author(s):  
Hiromi Yamashita ◽  
Hitoshi Takamura ◽  
Teruyoshi Matoba
Keyword(s):  
Protein Content ◽  
Near Infrared ◽  
Accurate Determination ◽  
Nir Spectroscopy ◽  
Amide Group ◽  
Nitrogen Compounds ◽  
Protein Nitrogen ◽  
Peptide Bonds ◽  
Related Compounds

The significance of the absorption at 2170 nm due to peptide bonds for the determination of protein content by near infrared (NIR) spectroscopy was evaluated by comparing it with absorptions due to other nitrogens (non-peptide nitrogens in protein and non-protein nitrogens). The amide group (asparagine and glutamine), guanido group (arginine), imidazole group (histidine) and amino group (lysine) in proteins did not exhibit absorption at 2170 nm. The absorptions of nucleic acid related compounds also were not observed at 2170 nm. These results suggest that a wavelength of 2170 nm is suitable for the accurate determination of protein content in foods.

scholarly journals Determination of Relative Stabilities of Metal‐Peptide Bonds in the Gas Phase

2021 ◽  
Author(s):  
Monika Cziferszky ◽  
Dianna Truong ◽  
Christian G. Hartinger ◽  
Ronald Gust
Keyword(s):  
Gas Phase ◽  
Peptide Bonds ◽  
Relative Stabilities
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