The Role of the Single Tryptophan Residue in the Structure and Function of Ribonuclease T1i1
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/92/1/143/7555175/92-1-143.pdf
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1. i-Motifs are more stable than G-quadruplexes in a hydrated ionic liquid;Chemical Communications;2015
2. New Insights into Transcription Fidelity: Thermal Stability of Non-Canonical Structures in Template DNA Regulates Transcriptional Arrest, Pause, and Slippage;PLoS ONE;2014-03-03
3. Mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase;Free Radical Biology and Medicine;2004-12
4. Trp59 to Tyr substitution enhances the catalytic activity of RNase T1 and of the Tyr to Trp variants in positions 24, 42 and 45;"Protein Engineering, Design and Selection";1993
5. Chemical modification of tryptophan residues and stability changes in proteins;Biochemistry;1990-10
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