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Author10 Posts
  #1

1. A protein contains a 30-amino acid structural motif with four cysteine residues coordinated to a zinc atom. In which of the following is this structured motif most likely to be found?


A. Nucleosome

B. Ribonuclease

C. Ribosome

D. Spliceosome

E. Transcription factor


Explain! and relate to other kind of structures with similar function.


  #2

E.......

  #3

E
The zinc finger domain is a DNA-binding motif consisting of specific spacings of cysteine and histidine residues that allow the protein to bind zinc atoms. The metal atom coordinates the sequences around the cysteine and histidine residues into a finger-like domain. The finger domains can interdigitate into the major groove of the DNA helix. The spacing of the zinc finger domain in this class of transcription factor coincides with a half-turn of the double helix. The classic example is the RNA pol III transcription factor, TFIIIA. Proteins of the steroid/thyroid hormone family of transcription factors also contain zinc fingers.



  #4

Transcription factor

  #5

E. Transcription factor




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  #6

E. Transcription factor




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... Idle hands are the DeVilS play ground ...

  #7

Which has the Leucine Zipper .. ? wink

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  #8

There was a question in either F1 or 2 which stated there is a protein with a disulfide bond, where in the cell is it found? Does someone remember this? what are they refering to

  #9

Pal, you have to have more specific than this, tons of proteins have disulfide bonds.

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  #10

I remember that question whournameiz, I chose extracelularly. I though they where refering to an Ig.

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