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Literature summary for 4.6.1.18 extracted from

  • Schnell, C.; Scharnagl, C.; Friedrich, J.
    Hole burning spectroscopy of ribonuclease A (2006), Phys. Chem. Chem. Phys., 8, 1315-1320.
    View publication on PubMed

Application

Application Comment Organism
analysis pressure tuning hole burning experiments using the UV-absorbing tyrosine residues. Ribonuclease A protein stays intact upon cooling to 2 K. Its various tyrosine sites show characteristic features which can be resolved in pressure tuning hole burning spectra. Reducing the sulfur bridges leads to a loss of the individual features, and the sites become alike. The respective compressibility is reduced by more than a factor of 2 and comes close to the value of free tyrosine in solution. Compared to the reduction of the sulfur bridges, the influence of guanidinium hydrochloride on the pressure tuning behavior is less pronounced Bos taurus

Crystallization (Commentary)

Crystallization (Comment) Organism
pressure tuning hole burning experiments using the UV-absorbing tyrosine residues. Ribonuclease A protein stays intact upon cooling to 2 K. Its various tyrosine sites show characteristic features which can be resolved in pressure tuning hole burning spectra. Reducing the sulfur bridges leads to a loss of the individual features, and the sites become alike. The respective compressibility is reduced by more than a factor of 2 and comes close to the value of free tyrosine in solution. Compared to the reduction of the sulfur bridges, the influence of guanidinium hydrochloride on the pressure tuning behavior is less pronounced Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
commercial preparation
-

Source Tissue

Source Tissue Comment Organism Textmining
pancreas
-
Bos taurus
-