Which of the following is not correct regarding protein domains or modules such as theimmunoglobulin domain, growth factor domain, and fibronectin domain?each type of domain is found in a variety of proteinsO they always have the same function in differend proteinsO domains are hypically 40 to 100 amine acids in lengthO they can be present in multiple copies in the same proteindomains of a certain type usuaily have the same tertiary structure

Amino acids when combined with a peptide bond, they form proteins. Proteins are macromolecules made…

Answered: Which of the following is not correct…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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You have digested a small protein with two different proteases, each protease acting on the protein in separate reactions. These are the peptide fragments generated: Trypsin: IPVK: Ile-Pro-Val-Lys ALEL: Ala-Leu-Glu-Leu HRPGDR: His-Arg-Pro-Gly-Asp-Arg FGADAEDGAMNK: Phe-Gly-Ala-Asp-Ala-Glu-Asp-Gly-Ala-Met-Asn-Lys YLEFISECIIQVLQSK: Tyr-Leu-Glu-Phe-Ile-Ser-Glu-Cys-Ile-Ile-Gln-Val-Leu-Gln-Ser-Lys Chymotrypsin: (Reaction conditions were used to maximize cutting to the C-terminal size of F, W, and Y.) LEF: Leu-Glu-Phe IPVKY: Ile-Pro-Val-Lys-Tyr GADAEDGAMNKALEL: Gly-Ala-Asp-Ala-Glu-Asp-Gly-Ala-Met-Asn-Lys-Ala-Leu-Glu-Leu ISECIIQVLQSKHRPGDRF: Ile-Ser-Glu-Cys-Ile-Ile-Gln-Val-Leu-Gln-Ser-Lys-His-Arg-Pro-Gly-Asp-Arg-Phe I am not sure what these questions are asking.
A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin and the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn—Tyr—Asp—Met—Phe—Ala—Arg Asp—Trp—Asn—Arg Gln—Met—Tyr—Cys—Pro—Ile—Arg Gln—Cys Cyanogen bromide treatment Tyr—Cys—Pro—Ile—Arg—Asn—Tyr—Asp—Met Asp—Trp—Asn—Arg—Gln—Met Phe—Ala—Arg—Gln—Cys
The folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu residues. What do these amino acids have in common? Why do they disrupt IDPs?
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
GLUT1 is a type III integral membrane protein with 12 amphipathic helices that span the cell membrane. Which amino acid side chains from the following amino acid sequence are most likely to form the hydrophobic (non-polar) face of an amphipathic alpha helix? -Ser-Leu-Val-Thr-Asn-Phe-Ile- 094 1 Select one: 5 4 W 7 2 6 3 DRO 10:00
Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in
A researcher has synthesized two peptides and needs to confirm whether the peptides were synthesized with the correct sequence using mass spectrometry. What is the sequence of the b4 and y7 ions for peptide GAMECHANGER? The peptide SLISRAEFLAGVRVGV is digested with trypsin. Then the products of the digestion are subjected to ESI TOF-MS in positive ion mode with the peptides in a pH 2 solution. What peptide fragments will result and what are their m/z?
Which amino acid sequence will form part of which protein structure, and why? Sequence 1: Ser-Phe-Gln-Val-Lys-Leu-His-Tyr-Asp-Val Sequence 2: Glu-Tyr-Leu-Asn-Phe-Ala-Gln-Val-Leu-Arg __Amphipathic beta strand __ Amphipathic alpha helix

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