Proteins Quiz - cloudfront.net
... 5. The specific interaction and orientation of the subunits of a large protein refer to its _____ structure. a) primary b) secondary c) tertiary d) quaternary ...
... 5. The specific interaction and orientation of the subunits of a large protein refer to its _____ structure. a) primary b) secondary c) tertiary d) quaternary ...
0101BWhat characterizes a prokaryotic cell
... __89) Which of the statements regarding enzymes is false? a) Enzymes are proteins that function as catalysts. b) Enzymes display specificity for certain molecules to which they attach. c) Enzymes provide activation energy for the reactions they catalyze. d) The activity of enzymes can be regulated. ...
... __89) Which of the statements regarding enzymes is false? a) Enzymes are proteins that function as catalysts. b) Enzymes display specificity for certain molecules to which they attach. c) Enzymes provide activation energy for the reactions they catalyze. d) The activity of enzymes can be regulated. ...
Population Genetics
... amino acid phenylalanine (see genetic code table) and only phenylalanine to the site of protein synthesis. • When a tRNA has its specific amino acid attached it is said to be “charged.” ...
... amino acid phenylalanine (see genetic code table) and only phenylalanine to the site of protein synthesis. • When a tRNA has its specific amino acid attached it is said to be “charged.” ...
Cellular Respiration
... NADH and FADH2 release electrons and their H+ ions This turns them into NAD+ and FAD H+ ions are sequestered in the inner mitochondrial space H+ ions diffuse down their concentration gradient through ATP synthase Oxygen is the final electron acceptor molecule in the ETC The maximum amount of ATP pro ...
... NADH and FADH2 release electrons and their H+ ions This turns them into NAD+ and FAD H+ ions are sequestered in the inner mitochondrial space H+ ions diffuse down their concentration gradient through ATP synthase Oxygen is the final electron acceptor molecule in the ETC The maximum amount of ATP pro ...
The Chemistry of Biology
... 31. Which of the following functional groups is mismatched to the organic compound? A. Phosphate-carbohydrates B. Sulfhydryl-proteins C. Amino-proteins D. Hydroxyl-alcohols E. Carboxyl-fatty acids 32. Organic chemicals always have a basic framework of the element _____ bonded to other atoms. A. Car ...
... 31. Which of the following functional groups is mismatched to the organic compound? A. Phosphate-carbohydrates B. Sulfhydryl-proteins C. Amino-proteins D. Hydroxyl-alcohols E. Carboxyl-fatty acids 32. Organic chemicals always have a basic framework of the element _____ bonded to other atoms. A. Car ...
... the smallest unit of matter that cannot normally be broken into smaller particles the process of breaking down large fat droplets into smaller fat droplets the loose association of amino acids in a polypeptide chain with each other, usually through H-bonds. e.g. alpha helix, beta pleated sheet the l ...
5 The structure and function of large biological molecules
... It has 4 valence electrons It can form up to 4 covalent bonds These can be single, double, or triple cov. Bonds It can form large molecules. These molecules and be chains, ring-shaped, or branched ...
... It has 4 valence electrons It can form up to 4 covalent bonds These can be single, double, or triple cov. Bonds It can form large molecules. These molecules and be chains, ring-shaped, or branched ...
Intermediary metabolism
... • synthesis of citrulline (used in urea cycle): intake of proteins in a diet (fed state) degradation of body proteins (starvation) concentration of glutamine ...
... • synthesis of citrulline (used in urea cycle): intake of proteins in a diet (fed state) degradation of body proteins (starvation) concentration of glutamine ...
Athena, Jen and Natalie`s Powerpt
... Aminoacyl tRNA synthetase Binds one amino acid to the tRNA tRNA also has an anticodon This complements the mRNA codon If the codon transcribed was AUG The anticodon would be UAC Methionine tRNA is in the P site A second tRNA enters the A site The 2 amino acids then peptide bind To begin the formati ...
... Aminoacyl tRNA synthetase Binds one amino acid to the tRNA tRNA also has an anticodon This complements the mRNA codon If the codon transcribed was AUG The anticodon would be UAC Methionine tRNA is in the P site A second tRNA enters the A site The 2 amino acids then peptide bind To begin the formati ...
Chapter 9
... •There are thousands of copies of the ETC in every mitochondrion due to the extensive folding of cristae membrane. The ETC carries electrons delivered by NAD and FAD from glycolysis and the Krebs cycle to oxygen, the final electron acceptor, through a series of redox reactions. In a redox reaction, ...
... •There are thousands of copies of the ETC in every mitochondrion due to the extensive folding of cristae membrane. The ETC carries electrons delivered by NAD and FAD from glycolysis and the Krebs cycle to oxygen, the final electron acceptor, through a series of redox reactions. In a redox reaction, ...
Multiple Choice:
... 26. C Resonance of the double bond between the carbonyl (C=O) and amide (C-N) bonds imparts a partial double bond character to the peptide (or amide) bond. Atoms that are bound even by a partial double bond cannot rotate with respect to each other, so the C, O, N, and H atoms of the peptide bond are ...
... 26. C Resonance of the double bond between the carbonyl (C=O) and amide (C-N) bonds imparts a partial double bond character to the peptide (or amide) bond. Atoms that are bound even by a partial double bond cannot rotate with respect to each other, so the C, O, N, and H atoms of the peptide bond are ...
Chapter 3 Protein Synthesis
... mRNA – messenger RNA: long single strand molecule, made in the nucleus during transcription, it travels to the ribosome and provides a code to manufacture proteins tRNA – transfer RNA: cross shaped molecule carrying an amino acid on one end and the “anti codon” on the other end. rRNA ...
... mRNA – messenger RNA: long single strand molecule, made in the nucleus during transcription, it travels to the ribosome and provides a code to manufacture proteins tRNA – transfer RNA: cross shaped molecule carrying an amino acid on one end and the “anti codon” on the other end. rRNA ...
Protein Unit Study Guide/Review Sheets
... If you have questions, make sure to ask them. Stop in before or after school. Review questions: 1. What elements comprise proteins? C, H, O, N 2. Are proteins organic? YES – CONTAIN CARBON AND HYDROGEN, THE REQUIREMENT FOR BEING AN ORGANIC MOLECULE 3. What is the name of the monomer of proteins? AMI ...
... If you have questions, make sure to ask them. Stop in before or after school. Review questions: 1. What elements comprise proteins? C, H, O, N 2. Are proteins organic? YES – CONTAIN CARBON AND HYDROGEN, THE REQUIREMENT FOR BEING AN ORGANIC MOLECULE 3. What is the name of the monomer of proteins? AMI ...
Basic Chemistry
... number of chemicals called buffers, which are present in body fluids. • Buffer - a substance or substances that help to stabilize the pH of a solution. ...
... number of chemicals called buffers, which are present in body fluids. • Buffer - a substance or substances that help to stabilize the pH of a solution. ...
Necessary Components for Translation
... • Ribosome is the site of protein synthesis. • Facilitates coupling of mRNA to tRNA. • Huge molecule: Large and small subunits must assemble for translation. • Ribosome composition: 60% rRNA and 40% protein • Transfer RNA (tRNA) Carries Amino Acids to the Growing Polypeptide Chain ...
... • Ribosome is the site of protein synthesis. • Facilitates coupling of mRNA to tRNA. • Huge molecule: Large and small subunits must assemble for translation. • Ribosome composition: 60% rRNA and 40% protein • Transfer RNA (tRNA) Carries Amino Acids to the Growing Polypeptide Chain ...
Lecture 6
... 3. The Lone Pair of the alcohol oxygen can react with the carbonyl carbon to set the whole thing in motion 4. Remember your VSEPR Geometry ...
... 3. The Lone Pair of the alcohol oxygen can react with the carbonyl carbon to set the whole thing in motion 4. Remember your VSEPR Geometry ...
Slide 1
... • Hydrolyze peptides • In microvillus • A dipeptidase hydrolyzes a dipeptide • 2 molecules of amino acids • Requires Mn • Zn as co factor ...
... • Hydrolyze peptides • In microvillus • A dipeptidase hydrolyzes a dipeptide • 2 molecules of amino acids • Requires Mn • Zn as co factor ...
Examination questions
... 45. Detoxification of ammonia (the ureosynthetic cycle, glutamine, glutamate). 46. Glucogenic and ketogenic amino acids ("families" according to the resulting amphibolic intermediates, reversible interconversions of amino acids, essential amino acids). 47. Metabolism of dicarboxylic amino acids. 48. ...
... 45. Detoxification of ammonia (the ureosynthetic cycle, glutamine, glutamate). 46. Glucogenic and ketogenic amino acids ("families" according to the resulting amphibolic intermediates, reversible interconversions of amino acids, essential amino acids). 47. Metabolism of dicarboxylic amino acids. 48. ...
Solutions to 7.012 Problem Set 1
... a) What is the primary structure of a protein? What force or forces (covalent bonds, ionic bonds, hydrogen bonds, or van der Waals forces) are involved in primary structure? The primary structure of a protein is the linear sequence of the amino acids. Covalent bonds link the individual amino acids b ...
... a) What is the primary structure of a protein? What force or forces (covalent bonds, ionic bonds, hydrogen bonds, or van der Waals forces) are involved in primary structure? The primary structure of a protein is the linear sequence of the amino acids. Covalent bonds link the individual amino acids b ...
BIOCHEMISTRY I Spring 2013 (General medicine, Dental
... 45. Detoxification of ammonia (the ureosynthetic cycle, glutamine, glutamate). 46. Glucogenic and ketogenic amino acids ("families" according to the resulting amphibolic intermediates, reversible interconversions of amino acids, essential amino acids). 47. Metabolism of dicarboxylic amino acids. 48. ...
... 45. Detoxification of ammonia (the ureosynthetic cycle, glutamine, glutamate). 46. Glucogenic and ketogenic amino acids ("families" according to the resulting amphibolic intermediates, reversible interconversions of amino acids, essential amino acids). 47. Metabolism of dicarboxylic amino acids. 48. ...
Biochemistry
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Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and relating to living organisms. By controlling information flow through biochemical signaling and the flow of chemical energy through metabolism, biochemical processes give rise to the complexity of life. Over the last decades of the 20th century, biochemistry has become so successful at explaining living processes that now almost all areas of the life sciences from botany to medicine to genetics are engaged in biochemical research. Today, the main focus of pure biochemistry is in understanding how biological molecules give rise to the processes that occur within living cells, which in turn relates greatly to the study and understanding of whole organisms.Biochemistry is closely related to molecular biology, the study of the molecular mechanisms by which genetic information encoded in DNA is able to result in the processes of life. Depending on the exact definition of the terms used, molecular biology can be thought of as a branch of biochemistry, or biochemistry as a tool with which to investigate and study molecular biology.Much of biochemistry deals with the structures, functions and interactions of biological macromolecules, such as proteins, nucleic acids, carbohydrates and lipids, which provide the structure of cells and perform many of the functions associated with life. The chemistry of the cell also depends on the reactions of smaller molecules and ions. These can be inorganic, for example water and metal ions, or organic, for example the amino acids which are used to synthesize proteins. The mechanisms by which cells harness energy from their environment via chemical reactions are known as metabolism. The findings of biochemistry are applied primarily in medicine, nutrition, and agriculture. In medicine, biochemists investigate the causes and cures of disease. In nutrition, they study how to maintain health and study the effects of nutritional deficiencies. In agriculture, biochemists investigate soil and fertilizers, and try to discover ways to improve crop cultivation, crop storage and pest control.