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Zinc fingers were first identified in a study of transcription in the African clawed frog, Xenopus laevis in the laboratory of Aaron Klug.A study of the transcription of a particular RNA sequence revealed that the binding strength of a small transcription factor (transcription factor IIIA; TFIIIA) was due to the presence of zinc-coordinating finger-like structures. [6]
Schellman loops incorporate a three amino acid residue RL nest (protein structural motif), [12] [13] in which three mainchain NH groups (from Schellman loop residues i+3 to i+5) form a concavity for hydrogen bonding to carbonyl oxygens. About 2.5% of amino acids in proteins belong to Schellman loops.
The image shows D (Q) spectra from a multifractal analysis of binary images of non-, mono-, and multi-fractal sets. As is the case in the sample images, non- and mono-fractals tend to have flatter D (Q) spectra than multifractals. The generalized dimension also gives important specific information.
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The tripartite motif is always present at the N-terminus of the TRIM proteins. The TRIM motif includes the following three domains: [1] (1) a RING finger domain (2) one or two B-box zinc finger domains when only one B-box is present, it is always a type-2 B-box; when two B-boxes are present the type-1 B-Box always precedes the type-2 B-Box
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