FALL 2016
Gene Organization and Expression – 410.610.82
Exam I
Johns Hopkins University
Zanvyl Krieger School of Arts and Sciences
Advanced Academic Programs This exam is an open-book, open-note exam. You will have one week to complete the questions. You must submit through the assignment in the Lesson. Late submissions will be penalized 10% for the first day and 20% each day after. Answer both questions on the exam. You can use all resources available to you to research these questions, but your answers must be yours and yours alone.
Style: Pretend you are at the front of the class and I have asked you these questions. Imagine how you would say the answer out loud.
Do not quote! You can’t memorize quotes; you’re in front of the class.
Do not cite literature! This isn’t a paper, it’s an answer to a question I’ve asked you.
Each answer should fit in on a single page, single space or two page, double space using 12 pt. font (you may delete the question)!
Good Luck!
1. Compare the characteristics of
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The concept of protein domains and motifs has dominated the first half of this course. Discuss the relevance of protein domains to the following topics:
a) binding of proteins to DNA
Domains are parts of proteins that have some known structure and functionality. Therefore, DNA binding are stretches of a protein that contains some known structural motif and has a high affinity for DNA allowing the two to bind.
One example of a proteins domain that binds DNA is the zinc finger which appear more than any other protein in eukaryotes. Zinc fingers are named for their finger-like appearance and can bind not only zinc, iron and other metals but also DNA, RNA and others.
Another example is the leucine zipper which gets its name from the pattern-like occurrence of leucine throughout the protein’s two α helices. Leucine zippers bind to promoters and induce transcription, ultimately expressing the gene.
b) binding of proteins to other
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DNA replication is an intricate process that requires many different proteins. Each protein preforms a very specific function in the creation of a new DNA strand. First helicase works by unwinding or dividing the original double helix into single stands. The point where the DNA is separated by the helicase is known as the replication fork. Single strand binding proteins attach to the newly made single strand of DNA to prevent re-annealing. Next is the addition of an RNA
The functional groups are called aminos and carboxyls. The linkage type is by using a peptide bond. The primary function of protein is build and repairs the body.
Length: By the time you answer each question, you should have 5 solid paragraphs, or about 2 and 2 ½ -3 pages double spaced. If you are looking for a word count, I would like 600+ words.
Three of the four questions below will appear on the exam and you will be asked to address all three. Maximum: Three sentences for each question.
Read each of the following short essay questions. Answer each question as descriptively as you can and be sure to use specific terms when applicable. Answers should be in complete sentences, with proper spelling & grammar. Point values vary per question.
answers will be marked as zero. Please include your answers to the Part A multiple-choice questions with your answer to
Step 1: Type your answers underneath each of the questions below and save the document.
Step 1: Type your answers underneath each of the questions below and save the document.
These proteins differ depending on their function in the cell, but often prevent misfolding of nascent protein, and assist in refolding of the misfolded proteins. Protein folding is dependent on the amino acid sequence within the polypeptide chain that is synthesized from the DNA strand in the ribosome.2 Upon release from the ribosome, the polypeptide chain undergoes a series of conformational changes based on the amino acid sequence to produce a functional protein structure. The assembled native protein is directed to the ER via vesicle
Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.
For the second part of the experiment, one had to use the knowledge learn from viewing protein molecules in FirstGlance in Jmol to analyze the protein PDB ID: 4EEY. The analysis of this protein was done using the RSCB protein data bank (PDB) at (http://www.rcsb.org/pdb/home/home.do).2
Campbell and Farrell define proteins as polymers of amino acids that have been covalently joined through peptide bonds to form amino acid chains (61). A short amino acid chain comprising of thirty amino acids forms a peptide, and a longer chain of amino acids forms a polypeptide or a protein. Each of the amino acids making up a protein, has a fundamental design that comprises of a central carbon or alpha carbon that is bonded to a hydrogen element, an amino grouping, a carboxyl grouping, and a unique side chain or the R-group (Campbell and Farrell 61).