Concept explainers
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
The Principle of Molecular Recognition Through Structural Complementarity
To explain:
How proteins interact with various biomolecules through molecular surfaces which are structurally complementary.
Introduction:
Proteins are made up of amino acids. Diversity of these amino acids is the key feature that enable proteins to interact with other biomolecules with various kinds of characteristics. Some amino acids are nonpolar (alanine, cysteine, glycine, isoleucine, leucine); they are very important in forming hydrophobic interactions. There are polar amino acids (serine, threonine, cysteine, asparagine, glutamine, and tyrosine); they involve in dipole-dipole interactions and H bonding. These polar amino acids are very important in forming interactions with polar carbohydrates. There are charged amino acids depending on the physiochemical pH value.
Explanation of Solution
Structural features that are formed as a result of diversity of the building blocks (amino acid) of proteins enable them to form interactions with various kinds of chemical species. For an example lysine and arginine (+ charge), aspartate and glutamate (- charge) can get charged based on the pH value of the medium. Thus, they can interact with charged species. Nucleic acids consist of pentose sugars, phosphate groups and nitrogenous bases. In general, nucleic acids interact with proteins forming various deferent interactions that includes hydrogen bonding, electrostatic interactions as well as dipole-dipole interactions.
When a protein is made up with the incorporation of various amino acids, they provide unique structural properties for the protein. Thus, they can interact with various biomolecules through these structural features.
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Chapter 1 Solutions
Biochemistry
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Interpreting Kinetics Experiments from Graphical Patterns The following graphical patterns obtained from kinetic experiments have several possible interpretations depending on the nature of the experiment and the variables being plotted. Give at least two possibilities for each.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. (Research Problem) The Nature and Roles of Linear Motifs in Proteins In addition to domains and modules, there are other significant sequence patterns in proteins—known as linear motifs—that are associated with a particular function. Consult the biochemical literature to answer the following questions: 1. What are linear motifs? 2. How are they different from domains?. 3. What are their functions? 4. How can they be characterized? 5. There are several papers that are good starting points for this problem. Neduva, V., and Russell, R., 2005. Linear motifs: evolutionary interaction switches. FEBS Letters 579:3342-3345. Gibson, T., 2009. Cell regulation: determined to signal discrete cooperation. Trends in Biochemical Sciences 34:471-482. Diella, K. Haslam, N., Chica., C. et aL, 2009. Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Frontiers of Bioscience 13:6580-6603.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Proteins and nucleic acids are informational macromolecules. What are the two minimal criteria for a linear informational polymer?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. To fully appreciate the elements of secondary structure in proteins, it is useful to have a practical sense of their structures. On a piece of paper, draw a simple but large zigzag pattern to represent a -strand. Then fill in the structure, drawing the locations of the moms of the chain on this zigzag pattern. Then draw a simple, large coil on a piece of paper to represent an -helix. Then fill in the structure, drawing the backbone atoms in the correction locations along the coil and indicating the locations of the R groups in your drawing.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Structural complementarity is the key to molecular recognition, a lesson learned in Chapter 1. The principle of structural complementarity is relevant to answering problems 5, 6, 7,11, 12, and 19. The quintessential example of structural complementarity in all of biology is the DNA double helix. What features of the DNA double helix exemplify structural complementarity?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Oligonucleotide Structure Draw the chemical structure of pACG.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Evaluation of -Helices in Proteins The hem agglutinin protein in influenza virus contains a remarkably long -helix, with 53 residues. How long is this -helix (in nm)? How many turns does this helix have? The typical residue in an -helix is involved in two H bonds. How many H bonds are present in this helix?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Cells as Steady-State Systems Describe what is meant by the phrase "cells tire steady-state systems." (Section 1.4)arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of a decapeptide revealed the presence of the following products: The following facts were observed: Neither car boxy peptidase A nor B treatment of the- decapeptide had any effect. Trypsin treatment yielded two tetrapcptides and free Lys. Clostripain treatment yielded a tetrapcptide and a hexapeptidc. Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes). Chymotrypsin treatment yielded two tripeptides and a telrapeptide. The N-terminal chymotryptic peptide had a net charge of — 1 at neutral pi I and a net charge of —3 al pH 12. One cycle of Ed man degradation gave the PTH derivative What is the ammo acid sequence of this decapeptide?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. (Historical Context) The Third Person of the -Helix Publication Who was Herman Branson? What was his role in the elucidation of the structure of the or-helix'.' Did he receive sufficient credit and recognition for his contributions? And how did the rest of his career unfold? Do a Google search on Herman Branson to learn about his life, and read the article by David Eisenberg under Further Reading. You may also wish to examine the original paper by Pauling, Corey, and Branson, as well as the following Web site: http://www.pirns. org/sitelmisclclassicsl..shtml Pauling, L., Corey, R. B., and Branson, H. R., 1951. The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proceedings of the National Academy of Sciences, USA 37:235-240.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Writing Dissociation Equations for Amino Acids Write equations fur the ionic dissociations of alanine, glutamate, histidine, lysine, and phenylalanine.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. The Structure and Ionization Properties of Nucleotides Draw the principal ionic species of occurring at pH 2.arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning