The diffusion of macromolecules is slowed by collisions with other large molecules and structures. Why? It is an important type of regulation because it ensures that energy is not wasted by an organism producing molecules it does not need. Bring your club to Amazon Book Clubs, start a new book club and invite your friends to join, or find a club that’s right for you for free. Like its predecessors, Lehninger Principles of Biochemistry, Sixth Edition strikes a careful balance of current science and enduring concepts, incorporating a tremendous amount of new findings, but only those that help illustrate biochemistry’s foundational principles. Ans: From the structure of lysine, we can calculate its molecular weight (146); when it condenses (loses H2O, Mr = 18) to form a peptide bond, the resulting residue contributes 146 – 18 = 128 to the protein’s molecular weight. Ans: A polymorphic protein is one whose amino acid sequence varies among the human population. Proteins are constantly being synthesized in a living cell. Given this biochemical similarity, how is the structural and functional diversity of living things possible? Please try again. With this edition, students will encounter new information emerging from high throughput DNA sequencing, x-ray crystallography, and the manipulation of genes and gene expression, and other techniques. Ans: See the titration curve for glycine in Fig. A                                             B                                               C, 1  DVEKGKKIDIMKCS    HTVEKGGKHKTGPNLH          GLFGRKTGQAPGYSYT, 2  DVQRALKIDNNLGQ  HTVEKGAKHKTAPNVH         GLADRIAYQAKATNEE, 3  LVTRPLYIFPNEGQ      HTLEKAAKHKTGPNLH          ALKSSKDLMFTVINDD, 4  FFMNEDALVARSSN   HQFAASSIHKNAPQFH            NLKDSKTYLKPVISET. Check out our DMCA Policy. Your email address will not be published. (b)  size-exclusion (gel filtration) chromatography, Ans: (a) Ion-exchange chromatography separates proteins on the basis of their charges. Lehninger Principles of Biochemistry: 6th Edition. Please try again. Your email address will not be published. For amino acids with neutral R groups, at any pH below the pI of the amino acid, the population of amino acids in solution will have: Pages: 80–81        Difficulty: 2     Ans: A. Describe what you would do to determine the specific activity of this enzyme solution. Ans: Some mutations lead to the synthesis of an inactive or defective enzyme or other protein that can no longer carry out its proper function, which is thus harmful to the organism. The specialized instruments required were prohibitively expensive. Easy to understand, relevant illustrations, and helpful examples. electrostatic guidance from nucleic acid structure. (c)  Size-exclusion chromatography (gel filtration) experiments indicate the native protein has an apparent Mr of 160,000. This is important to maintain the flexibility needed in macromolecules. Name two functions of (a) proteins, (b) nucleic acids, (c) polysaccharides, (d) lipids. Reviewed in the United Kingdom on May 2, 2016. Ans:  Homologs are any members of a particular protein family, paralogs are two homologs present in the same species, and orthologs are are two homologs present in different species. Ans: Peptide bonds are stable because hydrolysis of peptide (or amide) bonds has a high activation energy and as a result occurs very slowly. ____(e)  will have the greatest light absorbance at 280 nm? Inhaltsverzeichnis. Protein 4 is the protein that shows the greatest overall homology to protein 1. By what route do they get into proteins? Like its predecessors, Lehninger Principles of Biochemistry, Sixth Edition strikes a careful balance of current science and enduring concepts, incorporating a tremendous amount of new findings, but only those that help illustrate biochemistry’s foundational principles. relates the unknown protein to a series of protein markers with known molecular weights. Briefly describe the five major groupings of amino acids. Reviewed in the United Kingdom on April 11, 2018, Reviewed in the United Kingdom on November 8, 2015, My niece is at uni so great for her studies, Reviewed in the United Kingdom on March 8, 2016, Reviewed in the United Kingdom on October 23, 2014. Also, the 6th edition, compared to my 2nd edition, is very cheap looking. In a conjugated protein, a prosthetic group is: Pages: 84–85        Difficulty: 1     Ans: A. Prosthetic groups in the class of proteins known as glycoproteins are composed of: For the study of a protein in detail, an effort is usually made to first: In a mixture of the five proteins listed below, which should elute second in size-exclusion (gel- filtration) chromatography? The reason is that its side chain ___________. increasing the energy of the transition state. I have both and they are EXACTLY the same, only the 5th has a much better quality. What is the difference, if any, between cytosol and cytoplasm? The chirality of an amino acid results from the fact that its a carbon: Of the 20 standard amino acids, only ___________ is not optically active. Mit der Nutzung dieser Web-Seiten erklären Sie sich damit einverstanden. The cell maintains a dynamic steady state in which the amount of each protein remains fairly constant at the level required under given conditions. There was a problem loading your book clubs. Ans: Only the imidazole ring of the histidine R group has a pKa near physiological pH (pKa = 6.0), which suggests that histidine may provide buffering power in intercellular and intracellular fluids. The three-dimensional structure of macromolecules is formed and maintained primarily through noncovalent interactions. Ans: Some examples are 4-hydroxyproline, 5-hydroxylysine, g-carboxyglutamate, N-methyllysine, desmosine, and selenocysteine. proline; forms a covalent bond with the amino group. A biochemist is attempting to separate a DNA-binding protein (protein X) from other proteins in a solution. Ans:  An asymmetric carbon has four different substituents attached, and cannot be superimposed on its mirror image—as a right hand cannot fit into a left glove. the individual bands become stained so that the isoelectric focus pattern can be visualized. Draw the structure of Gly–Ala–Glu in the ionic form that predominates at pH 7. David L. Nelson, University of Wisconsin-Madison, USA, The Foundations of Biochemistry PART I: STRUCTURE AND CATALYSIS Water Amino Acids, Peptides, and Proteins The Three-Dimensional Structure of Proteins Protein Function Enzymes Carbohydrates and Glycobiology Nucleotides and Nucleic Acids DNA-Based Information Technologies Lipids Biological Membranes and Transport Biosignaling PART II: BIOENERGETICS AND METABOLISM Bioenergetics and Biochemical Reaction Types Glycolysis, Gluconeogenesis, and the Pentose Phosphate Pathway Principles of Metabolic Regulation The Citric Acid Cycle Fatty Acid Catabolism Amino Acid Oxidation and the Production of Urea Oxidative Phosphorylation and Photophosphorylation Carbohydrate Biosynthesis in Plants and Bacteria Lipid Biosynthesis Biosynthesis of Amino Acids, Nucleotides, and Related Molecules Hormonal Regulation and Integration of Mammalian Metabolism PART III: INFORMATION PATHWAYS Genes and Chromosomes DNA Metabolism RNA Metabolism Protein Metabolism Regulation of Gene Expression. Mehr Informationen finden Sie in unserem, Naturwissenschaften, Medizin, Informatik, Technik, ICONPARC - we enable digital business B2B. Name two uncommon amino acids that occur in proteins. We always try to provide you the best download experience by using Google Drive links and other fast alternatives. two free amino and two free carboxyl groups. Ans: Near pH = 7, the carboxylic acid group (—COOH) will dissociate to become a negatively charged —COO– group, and the —NH2 amino group will attract a proton to become a positively charged —NH3+ group. The variants have little or no differences in the function or activity of the protein. Ans: Living organisms are open systems and exchange both matter and energy with their surroundings. Like its predecessors, Lehninger Principles of Biochemistry, Sixth Edition strikes a careful balance of current science and enduring concepts, incorporating a tremendous amount of new findings, but only those that help illustrate biochemistry’s foundational principles. List the types of noncovalent interactions that are important in providing stability to the three-dimensional structures of macromolecules. (See Fig. Only three other proteins (A, B, and C) are present. Which of the following statements about cystine is correct? Why is an asymmetric carbon atom called a chiral center? A) Hydrogen bonds account for the anomalously high boiling point of water. It is just a very dense and info-packed book, so a few more diagrams/less text packed per page would have helped me process the information better. Clear writing and illustrations…Clear explanations of difficult concepts…Clear communication of the ways in biochemistry is currently understood and practiced. Although this process is clearly spontaneous, the products are colder than the reactants. They are: All of the amino acids that are found in proteins, except for proline, contain a(n): Pages: 75–76        Difficulty: 3     Ans: C. Which of the following statements about aromatic amino acids is correct? Find out more about the programme. Ans: The cell wall provides a rigid, protective shell for the cell.