f212 biological molecules
... • The Polar R groups of proteins interact with water forming hydrogen bonds that face outwards, This creates a hydrophobic core to the molecule • When proteins are heated these bonds break, the tertiary structure changes and the protein does not function. • The destruction of shape or loss of functi ...
... • The Polar R groups of proteins interact with water forming hydrogen bonds that face outwards, This creates a hydrophobic core to the molecule • When proteins are heated these bonds break, the tertiary structure changes and the protein does not function. • The destruction of shape or loss of functi ...
Chapter 4 - Organic Chemistry, Biochemistry
... protein to change. This can be caused by changes in temperature, pH, or salt concentration. For example, acid causes milk to curdle and heat (cooking) causes egg whites to coagulate because the proteins within them denature. If the protein is not severely denatured, it may regain its normal structur ...
... protein to change. This can be caused by changes in temperature, pH, or salt concentration. For example, acid causes milk to curdle and heat (cooking) causes egg whites to coagulate because the proteins within them denature. If the protein is not severely denatured, it may regain its normal structur ...
of Glycolysis
... • Phosphofructokinase‐ major control point; first enzyme “unique” to glycolysis • Pyruvate kinase •Phosphofructokinase responds to changes in: • Energy state of the cell (high ATP levels inhibit) • H+ concentration (high lactate levels inhibit) • Availability of alternate fuels such as fatty acids, ...
... • Phosphofructokinase‐ major control point; first enzyme “unique” to glycolysis • Pyruvate kinase •Phosphofructokinase responds to changes in: • Energy state of the cell (high ATP levels inhibit) • H+ concentration (high lactate levels inhibit) • Availability of alternate fuels such as fatty acids, ...
chapter3_Sections 1
... • A group of atoms bonded to a carbon of an organic compound • Gives a specific chemical property such as polarity or acidity. The following table gives examples of functional groups. One example is a phosphate group, found on DNA and the energy molecule, ATP. ...
... • A group of atoms bonded to a carbon of an organic compound • Gives a specific chemical property such as polarity or acidity. The following table gives examples of functional groups. One example is a phosphate group, found on DNA and the energy molecule, ATP. ...
Biomolecules
... result of functional groups • Functional groups maintain chemical properties no matter where they occur • Polar molecules are hydrophilic • Nonpolar molecules are hydrophobic • The degree to which organic molecules interact with water affects their function • Hydroxyl group (-OH) is one of the most ...
... result of functional groups • Functional groups maintain chemical properties no matter where they occur • Polar molecules are hydrophilic • Nonpolar molecules are hydrophobic • The degree to which organic molecules interact with water affects their function • Hydroxyl group (-OH) is one of the most ...
Nucleic Acids
... Pepsin is an enzyme that helps break down proteins in the stomach during digestion. It works at a pH of 2! Trypsin is an enzyme that helps break down proteins as well. It works in the intestines with a pH of 8. Many snake venoms are enzymes that work when directly injected into blood or tissue (pH = ...
... Pepsin is an enzyme that helps break down proteins in the stomach during digestion. It works at a pH of 2! Trypsin is an enzyme that helps break down proteins as well. It works in the intestines with a pH of 8. Many snake venoms are enzymes that work when directly injected into blood or tissue (pH = ...
Understanding an Enzyme Active Site
... Protein secondary structure (alpha helices and beta sheets) provides that stable scaffolding upon which the critical active site amino acids can be precisely positioned in 3D space. The 2-3 amino acids that come together in 3D space to create an enzyme active site are very far apart in the linear se ...
... Protein secondary structure (alpha helices and beta sheets) provides that stable scaffolding upon which the critical active site amino acids can be precisely positioned in 3D space. The 2-3 amino acids that come together in 3D space to create an enzyme active site are very far apart in the linear se ...
Enzymes - Ústav lékařské chemie a biochemie
... f. With tubes 1 and 3 (where starch was used) also test for starch using Lugol solution (prediluted with water: 4 drops/10 ml of water). Evaluation: Indicate to the table in your lab report where the cleavage of the substrate occurred using symbols + (substrate cleaved) or − (substrate not cleaved). ...
... f. With tubes 1 and 3 (where starch was used) also test for starch using Lugol solution (prediluted with water: 4 drops/10 ml of water). Evaluation: Indicate to the table in your lab report where the cleavage of the substrate occurred using symbols + (substrate cleaved) or − (substrate not cleaved). ...
Problem Set 1 Solution
... f) Name the amino acid present in 1A3N that is substituted to Val6 in 2HBS. How does the nature of the side-chain of this amino acid differ from Val? Normal hemoglobin has glu6, which is substituted by val in 2HbS. The amino acid glu has a polar, hydrophilic side-chain in comparison to val6 which ha ...
... f) Name the amino acid present in 1A3N that is substituted to Val6 in 2HBS. How does the nature of the side-chain of this amino acid differ from Val? Normal hemoglobin has glu6, which is substituted by val in 2HbS. The amino acid glu has a polar, hydrophilic side-chain in comparison to val6 which ha ...
5_Bio_1_ReKaps
... Lock and Key: the enzyme and substrate fit together exactly (no longer the accepted theory) Induced Fit: the presence of the appropriate substrate causes a conformational change in the enzyme such that the enzyme and substrate fit together (the accepted theory) Reaction Energy Profiles: an enzym ...
... Lock and Key: the enzyme and substrate fit together exactly (no longer the accepted theory) Induced Fit: the presence of the appropriate substrate causes a conformational change in the enzyme such that the enzyme and substrate fit together (the accepted theory) Reaction Energy Profiles: an enzym ...
Bio160 ExIII Sp09
... d. enzymes lower the activation energy required for chemical reactions e. the reactants in an enzyme-catalyzed reactions are referred to as substrates 42. The substrate that is catalyzed by the enzyme we studied in our on-line enzyme lab is: a. glucose b. sucrose c. fructose d. invertase e. acarbose ...
... d. enzymes lower the activation energy required for chemical reactions e. the reactants in an enzyme-catalyzed reactions are referred to as substrates 42. The substrate that is catalyzed by the enzyme we studied in our on-line enzyme lab is: a. glucose b. sucrose c. fructose d. invertase e. acarbose ...
Chapter 13: Genetic Engineering
... 5. Plasmid is then returned to bacterium and reproduces with donor gene in it. Transgenic organism – organism with foreign DNA incorporated in its genome (genes) 6. Bacterium reproduces and starts producing human insulin gene which we harvest from them. ...
... 5. Plasmid is then returned to bacterium and reproduces with donor gene in it. Transgenic organism – organism with foreign DNA incorporated in its genome (genes) 6. Bacterium reproduces and starts producing human insulin gene which we harvest from them. ...
division - IRIS - Lake Land College
... Distinguish between glycogenesis and glycogenolysis. Determine the moles of ATP produced by the complete oxidation of a given fatty acid by way of B-oxidation and the citric acid cycle. Write equations to illustrate transamination and oxidative deamination of amino acids. Explain the role of carbohy ...
... Distinguish between glycogenesis and glycogenolysis. Determine the moles of ATP produced by the complete oxidation of a given fatty acid by way of B-oxidation and the citric acid cycle. Write equations to illustrate transamination and oxidative deamination of amino acids. Explain the role of carbohy ...
Carbon compounds - Sonoma Valley High School
... compounds that can be bonded together to form larger ones. • 3 important ones are: – sugars – amino acids ...
... compounds that can be bonded together to form larger ones. • 3 important ones are: – sugars – amino acids ...
Saliva Hook - BioScholars1st
... • Explain the function of the macromolecule and give an example of its importance to life • Examples of foods that contain the macromolecules: sugar, protein, starch and fat. Teacher Notes: Carbohydrates: simple sugar (glucose specifically) is the monomer monomers form starches, cellulose potatoes, ...
... • Explain the function of the macromolecule and give an example of its importance to life • Examples of foods that contain the macromolecules: sugar, protein, starch and fat. Teacher Notes: Carbohydrates: simple sugar (glucose specifically) is the monomer monomers form starches, cellulose potatoes, ...
Chem 150: Review for Ch
... -Can you tell what does Ala-Gly-Ser mean? Which is the N-terminal residue, C-terminal residue? How would you name this peptide? 13.4: Polypeptide and Protein - what is an oligopeptide? what is a polypeptide? How do you recognize a polypeptide? - what is a protein? Globular protein, fribrous protein ...
... -Can you tell what does Ala-Gly-Ser mean? Which is the N-terminal residue, C-terminal residue? How would you name this peptide? 13.4: Polypeptide and Protein - what is an oligopeptide? what is a polypeptide? How do you recognize a polypeptide? - what is a protein? Globular protein, fribrous protein ...
No Slide Title
... molecule at the beginning of photosynthesis. The water is split by solar energy. ...
... molecule at the beginning of photosynthesis. The water is split by solar energy. ...
Full size lecture slides (PDF file, 660 kB)
... hydrophobic and hydrophilic amino acids are • Once secondary structure has formed it folds back upon itself to form an even more stable molecule: tertiary structure. • If a protein consists of more than one amino acid chain, the arrangement of the subunits is called the quaternary structure ...
... hydrophobic and hydrophilic amino acids are • Once secondary structure has formed it folds back upon itself to form an even more stable molecule: tertiary structure. • If a protein consists of more than one amino acid chain, the arrangement of the subunits is called the quaternary structure ...
08_Lecture_Presentation_PC
... • Every chemical reaction between molecules involves bond breaking and bond forming • The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA) • Activation energy is often supplied in the form of thermal energy that the reactant molecu ...
... • Every chemical reaction between molecules involves bond breaking and bond forming • The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA) • Activation energy is often supplied in the form of thermal energy that the reactant molecu ...
Metabolism: Citric acid cycle
... 14. A. Use the figure of question 8 to write down the answers to the following questions. B. Indicate the enzymes that are inhibited by ATP. C. Indicate the enzymes that are inhibited by NADH. D. Indicate the enzymes that are feedback inhibited by succinyl CoA. E. Indicate the enzymes that are allos ...
... 14. A. Use the figure of question 8 to write down the answers to the following questions. B. Indicate the enzymes that are inhibited by ATP. C. Indicate the enzymes that are inhibited by NADH. D. Indicate the enzymes that are feedback inhibited by succinyl CoA. E. Indicate the enzymes that are allos ...
2nd Phase of Glycolysis
... In addition to the allosteric effectors, pyruvate kinase is regulated by covalent modification. Hormones such as glucagon activate a cAMP-dependent protein kinase which transfers the γphosphate of ATP to the pyruvate kinase. The phosphorylated pyruvate kinase is more strongly inhibited by ATP and a ...
... In addition to the allosteric effectors, pyruvate kinase is regulated by covalent modification. Hormones such as glucagon activate a cAMP-dependent protein kinase which transfers the γphosphate of ATP to the pyruvate kinase. The phosphorylated pyruvate kinase is more strongly inhibited by ATP and a ...
Nedd8 processing enzymes inSchizosaccharomyces pombe
... differences in Nedd8 substrates between these organisms. Just as ubiquitylation is reversed by ubiquitin isopeptidases, Nedd8 conjugation is reversed by Nedd8 isopeptidases in a process known as deneddylation. The best characterized deneddylating enzymes include the COP9 signalosome subunit Csn5 [11 ...
... differences in Nedd8 substrates between these organisms. Just as ubiquitylation is reversed by ubiquitin isopeptidases, Nedd8 conjugation is reversed by Nedd8 isopeptidases in a process known as deneddylation. The best characterized deneddylating enzymes include the COP9 signalosome subunit Csn5 [11 ...
MBP 1022, LECT 2 DAN_Oct22
... interactions, disulfide bonds, folding of domains Quarternary; applies to multimeric protein (2 polypep, noncovalent) The sequence of R-groups along the chain is called the primary structure. Secondary structure refers to the local folding of the polypeptide chain. Tertiary structure is the arrangem ...
... interactions, disulfide bonds, folding of domains Quarternary; applies to multimeric protein (2 polypep, noncovalent) The sequence of R-groups along the chain is called the primary structure. Secondary structure refers to the local folding of the polypeptide chain. Tertiary structure is the arrangem ...
CSM 101 Fall 2010 Timeline
... A reaction being spontaneous means that it will favor going toward products over reactants in standard conditions. Spontaneity depends on the Gibbs free energy of the reaction as well as the entropy change. A nonspontaneous reaction will have a positive Gibbs free energy and entropy decrease. This ...
... A reaction being spontaneous means that it will favor going toward products over reactants in standard conditions. Spontaneity depends on the Gibbs free energy of the reaction as well as the entropy change. A nonspontaneous reaction will have a positive Gibbs free energy and entropy decrease. This ...
Download PDF
... structure of proteins, and how this translates into differences in the function of these proteins. We will also examine the structures of DNA, RNA, and ribosomes, and how these structures are used in maintaining and communicating genetic information. We will also cover the synthesis of biopolymers – ...
... structure of proteins, and how this translates into differences in the function of these proteins. We will also examine the structures of DNA, RNA, and ribosomes, and how these structures are used in maintaining and communicating genetic information. We will also cover the synthesis of biopolymers – ...
Enzyme
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.