Characterization of the tryptophan residues of human placental ribonuclease inhibitor and its complex with bovine pancreatic ribonuclease A by steady-state and time-resolved emission spectroscopy

Article Abstract:

A study on human placental ribonuclease inhibitor (hRI) containing six tryptophan (Trp) residues located at positions 19, 261, 263, 318, 375, and 438 and its complex with RNase A is conducted using steady-state and time-resolved fluorescence (298 K) as well as low-temperature phosphorescence (77 K). The accessible surface area values of Trp residues in the wild-type hRI and its complex and consideration of inter-Trp energy transfer in the wild-type hRI reveal that one of the Trp residues is Trp19, which is located in hydrophobic buried region.

Usage, Ribonuclease, Emission spectroscopy, Atomic emission spectroscopy

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Low-temperature study of photoinduced energy transfer from tryptophan residues of Escherichia coli alkaline phosphatase to bound terbium

Article Abstract:

Low-temperature phosphorescence (LTP) and zero-field-splitting (zfs) parameters of the lowest triplet state in zero magnetic field and triplet sublevel dynamics of tryptophan (Trp) residues in alkaline phosphatase (AP), metal-depleted AP (apoAP), and terbium-substituted AP (TbAP) are reported. The results are evaluated to find a plausible mechanism of energy transfer (ET) and TbAP at low temperature.

Escherichia coli, Alkaline phosphatase, Chemical properties, Terbium

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Band-shape analysis of decayed slow-passage ODMR in the photoexcited triplet state of tryptophan

Article Abstract:

The analysis of delayed slow passage optically detected magnetic resonance band shapes of the triplet state of tryptophan, lysyl-tryptophanyl-lysine, N-acetyl tryptophanamide, and ribonuclease T1 from A. oryzae in low-temperature aqueous glass is presented. The quality of the fit was generally satisfactory.

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