EC Number   |
General Information |
Reference |
|---|
   3.1.31.1 | more |
enzyme tryptophan fluorescence spectra, fluorescence measurements of protein unfolding under pressure, high-pressure fluorescence spectroscopy and single value decomposition analysis, overview |
729277 |
| 3.1.31.1 | more |
mannosylglycerate preferentially affects specific structural elements of the P117G/H124L/S128A mutant enzyme, structure analysis, overview |
730894 |
| 3.1.31.1 | more |
MNase mapping of the enhancer chromatin structure in the Drosophila melanogaster embryo to analyse chromatin structure in a developmental setting, and identification of structural changes on a cis-regulatory element targeted by the Knirps repressor, method development and optimization, overview |
717620 |
| 3.1.31.1 | more |
residue W140 is critical to SNase structure and function |
717382 |
| 3.1.31.1 | more |
sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview |
-, 730786 |
| 3.1.31.1 | more |
staphylococcal nuclease domain-containing 1, SND1, is a multifunctional nuclease containing four staphylococcal nuclease domains and a tudor domain. No potential interaction between enzyme SND1 and p65 subunit of NF-kappa B |
729981 |
| 3.1.31.1 | more |
the enzyme interacts with Argonaute protein PmAgo1, but not with PmAgo2 or PmAgo3. Interaction between PmAgo and the enzyme is mediated through the N-terminal domain of PmAgo1 and the SN1-2 domains of the enzyme, interaction analysis and mapping using the two-hybrid system for different protein constructs, overview |
729764 |
| 3.1.31.1 | more |
the fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model, overview. Method evaluation to distinguish a two-state from a three-state denaturation |
729335 |
| 3.1.31.1 | more |
the introduction of internal cavities into different subdomains affects local stability, flexibility, and dynamics of the enzyme, NMR spectroscopy under atmospheric and high pressure, H/D exchange and molecular dynamics simulations of wild-type and mutant enzymes, overview. Responses to the creation of cavities cannot be anticipated from global thermodynamic stability or crystal structures, they depend on the local structural and energetic context of the substitutions |
730910 |
| 3.1.31.1 | more |
thermodynamic parameters derived from urea-induced unfolding of mutant SNase140 and mutant SNase141 in comparison with those of wild-type SNase and mutant SNase140 in the presence of calcium, backbone dynamics, detailed overview. Mutant SNase140 unfolds easily compared to mutant SNase141 and wild-type SNase |
717245 |
