Which of the following protein is a glycoprotein as evidenced by the provided illustration and information only? }} Oll OI O III =GPI Anchor I and II I and III III

i. ii. i.v. 22. Using the figure below, answer the following questions. Identify 2 independent helices domains Identify a disordered region In the structure, box the cofactor and name it (abbreviation accepted) Using the figure, draw the structure of the cofactor bound to this protein

Proteins can be separated into 9 general classifications based on the role they play in a cell. List or briefly describe two of these functional classifications and provide an example of a protein that falls into each of those two categories.

Amino Acid 3-Letter 1-Letter Second letter Code Code Alanine Cysteine Aspartic acid or aspartate Glutamic acid or glutamate | Phenylalanine Glycine Histidine Ala Cys Asp Glu UCU Phe UGU cys UGC UUUT UAU Tyr UAC D UUC UC Ser UUA UAA Stop UGA Stop UAG Stop UGG Trp G UCA Phe Leu UUG UCG Gly G H. His Ile CUU CCU CAU CGU U His CAC CÚC Leu CUA CGC CGA Isoleucine Lysine Leucine Pro Arg Lys K CAA Gin CAG CCA Leu L. CUG CCG CG Methionine Met M AUU AUC le ACU) ACC AAU1 AAC AGU Asn Asparagine Proline Glutamine Arginine Serine Asn Ser AGC AGA Arg Pro P. Thr AAA Gln Arg Ser AUA ACA AUG Met ACG AAG Lys AGG R GUU) GCU) GAU1 GGU GGC Gly Threonine Valine Tryptophan Tyrosine Thr GUC Val GUA GCC Ala GCA Val V GAA GAG GGA W Trp Тут Glu GUG GCG GGG Y Apply all that you have learned to solve the following: If you have the following DNA sequence: 5-ATGGCIOTOGTATTAAATAG-3 1. What is the sequence of the bases in the complementary DNA strand in a 3' to 5 direction ?( NB" Just type the letter for the bases) 2.…

α-Keratin is an intermediate filament with a basic structural unit of two a helices in a coiled coil. Each helix has a seven-residue repeating unit (heptad repeat). A representation of the a helices of a coiled coil dimer is shown. Each letter represents a different amino acid residue. f g d e Review the table of amino acids. a d g f Identify the three true statements about the structure of keratin. ☐ The a helix of the coiled coil is wound less tightly than predicted for an α helix. ☐ Each polypeptide in the dimer has 3.6 residues per turn, and a nonpolar group occurs every 3.5 residues, resulting in a slight winding, or twist, around the other polypeptide, forming a coiled coil. Arg-Ala-His-Glu-His-Thr-Asp is a likely repeat in the a helix of keratin. ☐ Val-Thr-Asp-Ala-Glu-Arg-His is a likely repeat in the a helix of keratin. ☐ The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent. ☐ Keratin molecules are very strong due…

oligosaccharides are attached to proteins for a variety of reasons. They’re attached to the newly synthesized proteins in the endoplasmic reticulum and golgi apparatus to assign them destination labels, misfolded protein labels, and quality control labels. How does the polarity and charge of these oligosaccharides affect the protein they are bound to?

Non covalent bonds are very important in cell biology, could you explain why and provide an example that illustrates their importance ( do not chose protein folding as an example) What are the different levels of protein structure and what are the different parameters (sequence, type of bonds, etc...) that influence protein folding at these different levels?

A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypep- tide. Fragments are grouped according to size. Pentapeptide Fragments Tetrapeptide Fragments Phe-Val-Asn-Gln-His Gln-His-Leu-Cys His-Leu-Cys-Gly-Ser His-Leu-Val-Glu Gly-Ser-His-Leu-Val Leu-Val-Glu-Ala

Which of the following amino acids are more likely to be on the interior of the protein? And which are more likely to be exposed to the surface? L I D E W A V K H M Q Y

Disulfide linkages are uncommon in cytoplasmic proteins, whereas they are common in extracellular proteins. Why?