Alignment of protein sequences from the HOX gene family identifies a highly conserved domain in the C-terminal part of the protein that is a domain (one acronym and one word). Although Hox genes have important roles during embryogenesis and tissue differentiation, the different HOX proteins bind to very similar DNA (one word) that are rich in the bases and (one word each). To ensure high affinity binding to (one acronym) and specific regulation of target (one word), the HOX proteins form complexes with (two words).

Alignment of protein sequences from the HOX gene family identifies a highly conserved domain in the C-terminal part of the protein that is a domain (one acronym and one word). Although Hox genes have important roles during embryogenesis and tissue differentiation, the different HOX proteins bind to very similar DNA (one word) that are rich in the bases and (one word each). To ensure high affinity binding to (one acronym) and specific regulation of target (one word), the HOX proteins form complexes with (two words).

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter15: Genomes And Genomics

Section: Chapter Questions

Problem 13QP

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Alignment of protein sequences from the HOx gene family identifies a highly conserved domain in the C-terminal part of the protein that is a domain (one acronym and one word). Although Hox genes have important roles during embryogenesis and tissue (one word) that are rich in the bases (one word each). To ensure high affinity binding to and differentiation, the different HOX proteins bind to very similar DNA (one acronym) (one word). the HOX proteins form complexes with (two words). and specific regulation of target A Moving to another question will save this response. K Question 12 of 15
(c) By binding one L-tryptophan molecule/monomer, the trp repressor binds to DNA to suppress syn- thesis of L-tryptophan in E. coli. Below is the amino acid sequence of the helix – (reverse) turn – helix region of the trp repressor that binds to DNA compared to the sequence of the corresponding DNA binding motif of the Prl protein, a different type of repressor protein. A diagram of the trp repressor dimer is also shown. reverse turn trp helix 4 70 Trp -Gly-Glu-Met-Ser-Gln-Arg-Glu-Leu-Lys-Asn-Glu-Leu-Gly-Ala-Gly- Ile- Prl -Ser-Glu-Glu-Ala-Lys-Glu-Glu-Leu-Ala-Lys-Lys-Cys-Gly-Ile-Thr- Val- Pri heilix trp helix 5 80 90 Trp Ala-Thr-Ile-Thr-Arg-Gly-Ser sgn-Ser-Leu-Lys-Ala-Ala- Prl Ser-Gln-Val-Ser-Asn-Trp-Phe-Gly-Asn-Lys-Arg-Ile-Arg- Prl helix
The steroid progesterone has an important role in the female reproductive system. Researchers interested in studying membrane progestin receptors (MPRS) developed a method to produce and purify the protein in active form. First, the researchers devised a way to prepare a specific MPR known as hMPRA using the machinery of yeast cells. In order to facilitate purification and identification in later studies, they manipulated the yeast cells so that they attached two different tags to the C-terminal end of the protein. The first tag, Compound 1, is a peptide sequence that acts as an epitope, part of a much larger peptide sequence that is recognized by the immune system. The second sequence consisted of six consecutive histidine residues (His). This sequence binds tightly to Ni2+ cations. In chromatography, (His), tag labeled proteins can be eluted from Ni²+. supported columns by adding a small molecule to the eluent that mimics the side chain of histidine.…
The steroid progesterone has an important role in the female reproductive system. Researchers interested in studying membrane progestin receptors (MPRs) developed a method to produce and purify the protein in active form. First, the researchers devised a way to prepare a specific MPR known as hMPRA using the machinery of yeast cells. In order to facilitate purification and identification in later studies, they manipulated the yeast cells so that they attached two different tags to the C-terminal end of the protein. The first tag, Compound 1, is a peptide sequence that acts as an epitope, part of a much larger peptide sequence that is recognized by the immune system. The second sequence consisted of six consecutive histidine residues (His). This sequence binds tightly to Ni2+ cations. In chromatography, (His), tag labeled proteins can be eluted from Ni²+- supported columns by adding a small molecule to the eluent that mimics the side chain of histidine. After preparing hMPRA, the…
Consider the structure of Cro repressor protein from bacteriophage lambda E. It is a DNA binding protein, and like many sequence- specific DNA binding proteins, it must function as a homodimer Ex. Notice the mutual docking of a phenylalanine residue from each subunit into a hydrophobic pocket of the partner subunit. These hydrophobic interactions are required for dimerization. The noncovalent interactions highlighted in yellow are also required for dimerization. These interactions represent examples of: Osecondary structure O tertiary structure O quaternary structure O secondary AND quaternary structure Ⓒ tertiary AND quaternary structure
A double-stranded fragment of viral DNA, one of whose strands is shown below, encodes two peptides, called vir-1 and vir-2. Adding this double-stranded DNA fragment to an in vitro transcription and translation system yields peptides of 10 residues (vir-1) and 5 residues (vir-2). Solve, (b) Determine the amino acid sequence of each peptide.
A short RNA molecule was isolated that demonstrated a hyperchromicshift , indicating secondary structure. Itssequence was determined to be5'-AGGCGCCGACUCUACU-3'(a) Propose a two-dimensional model for this molecule.(b) What DNA sequence would give rise to this RNA moleculethrough transcription?(c) If the molecule were a tRNA fragment containing a CGA anticodon,what would the corresponding codon be?(d) If the molecule were an internal part of a message, whatamino acid sequence would result from it following translation?
EF-Tu binds all aminoacyl–tRNAs with approximately equal affinity so that it can deliver them to the ribosome with the same effi ciency. Based on the experimentally determined binding constants for EF-Tu and correctly charged and mischarged aminoacyl–tRNAs (see table), explain how the tRNA–EF-Tu recognition system could prevent the incorporation of the wrong amino acid during translation.
The sequence of the sense strand of a mammalian gene is (shown). Determine the sequences of the mature RNA and the encoded protein. Assume that transcription initiates at a G approximately 25 bp downstream of the TATAATA sequence, that each 5′ splice site has the sequence AG/GUAAGU, and that each 3′ splice site has the sequence CAG/G (where / marks the location of the splice).
High salt concentrations tend to cause protein aggregation. Suggest a way to identify proteins normally expressed in particular bacterial species that can retain their solubility despite high salt conditions.
Briefly discuss (referring to the images provided) why mutant 2 fails to produce functional protein. Note that none of the mRNA transcribed from this gene is of the expected size; some of the mRNA molecules produced are 223 nucleotides shorter than expected, whilst others are 47 nucleotides longer than expected.
If the following truncated peptide represents the active domain of the COVID19’s S-protein N-terminal ----Leu-Leu-Gly-Cys-Ile-Glu-Ser-Thr-Cys-Ala ------ C-terminal a) state the RNA sequence of this peptide given that Leu is the first amino acid b) show a point mutation using the RNA sequence & explain how it results in silent mutation effect c) show a deletion mutation using the RNA sequence & explain the consequence(s)