Helices are common secondary structures found in proteins. Choose two different protein helices and compare and contrast their key structural features. How do helices adapt to their structural environment in the protein? In Tansey Biochemistry, there are several examples / case studies of proteins that help us understand protein structure and function. Choose two different proteins from these examples and compare and contrast their key structural features. Briefly explain how their structures are adapted to their function

Helices are common secondary structures found in proteins. Choose two different protein helices and compare and contrast their key structural features. How do helices adapt to their structural environment in the protein? In Tansey Biochemistry, there are several examples / case studies of proteins that help us understand protein structure and function. Choose two different proteins from these examples and compare and contrast their key structural features. Briefly explain how their structures are adapted to their function

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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question 38 The constant region of each heavy chain determines the class of the heavy chain. True False
Question 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
QUESTION NO. 1 Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition particle (SRP). C. signal peptide is usually cleaved from the protein before the protein is inserted into the ER membrane. D. docking protein is actually an SRP receptor and serves to bind the SRP to the ER. E. SRP and docking protein do not enter the ER lumen but are recycledQUESTION NO. 2 All of the following statements about telomerase are correct except A. the RNA component acts as a template for the synthesis of a segment of DNA. B. it adds telomeric repeats to the 5'-ends of the DNA strands. C. it provides a mechanism for replicating the ends of linear…
QUESTION 22 The DNA sequences that are most conserved between human and mouse would most likely be located in: A Highly-repeated sequences, such as microsatellite regions B Highly repeated sequences, such as Alu sequences C Moderately-repeated non-coding sequences D Coding regions of single-copy genes
QUESTION NO. 1 Fragile X syndrome is a common form of inherited mental retardation. The mutation in the disease allows the increase of a CGG repeat in a particular gene from a normal of about 30 repeats to 200-1000 repeats. This repeat is normally found in the 5' untranslated region of a gene for the protein FMR1. FMR1 might be involved in the translation of brain-specific mRNAs during brain development. The consequence of the very large number of CGG repeats in the DNA is extensive methylation of the entire promoter region of the FMR1 gene. Methylation of bases in DNA usually A. facilitates the binding of transcription factors to the DNA. B. makes a difference in activity only if it occurs in an enhancer region. C. prevents chromatin from unwinding. D. inactivates DNA for transcription. E. results in increased production of the produce of whatever gene is methylated.QUESTION NO. 2 The best definition of an endonuclease is that it hydrolyzes A. nucleotide from…
QUESTION 16 Peptidyl transferase activity (peptide bond enzyme activity) is associated with what site in the ribosome? E P A X
Question 10 (2 points) A protein heterodimer would be considered an example of: -primary structure -secondary structure -tertiary structure -quaternary structure -atomic structure
Question 10. All of the following areparts of a nucleotide EXCEPT:A. a five-carbon sugar.B. a six-carbon sugar.C. a phosphate group.D. a nitrogenous base.
Question 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?
Question 15 Activities found in the rough ER and its functions include the folllowing EXCEPT provides a membrane binding site for the RNA with signal a signal sequence facilitates post-translational modifications allows the entry of polypeptides that will undergo glycosylation provides a membrane scaffold for binding of ribosomes for protein synthesis
Question 1: tRNA and amino acyl tRNA synthetases Part g: What chemical and structural characters are shared by the amino acids Ile, Val and Met? Part h: What enzyme attaches Ile to tRNA? Part i: Compare the frequency of the correct Ile entering the active site and the frequency of an incorrect amino acid entering the active site of this enzyme. Be specific with numbers. Part j: Compare the frequency of the correct tRNA(Ile) entering the active site and the frequency of an incorrect tRNA entering the active site of this enzyme. Be specific with numbers. Part k: Apply the Entropy change formula and multiply by T = 303 K (30 C) to determine the energetic cost of accurately attaching Ile to its cognate tRNA(Ile). Part l: Is there enough energy in the chemical transformation of ATP → AMP + 2Pi to pay this information cost?
Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSN