Enzyme kinetics - Study guides, Class notes & Summaries

structures and properties of amino acids Nonpolar, Aliphatic (Hydrophobic): Glycine (Gly, G) Alanine (Ala, A) Valine (Val, V) Leucine (Leu, L) Isoleucine (Ile, I) Proline (Pro, P) Aromatic (Hydrophobic): Phenylalanine (Phe, F) Tyrosine (Tyr, Y) Tryptophan (Trp, W) Polar, Uncharged (Hydrophilic): Serine (Ser, S) Threonine (Thr, T) Cysteine (Cys, C) Methionine (Met, M) Asparagine (Asn, N) Glutamine (Gln, Q) Positively Charged (Basic, Hydrophilic): Lysine (Lys, K) Arginin...

Spectroscopy Methods correct answers- Fluorescence Microscopy - super resolution microscopy - flow cytometry / mass cytometry Ligand binding can be tested by correct answers- equilibrium dialysis - Fluorescence (anisotropy) - FRET - SPR Enzyme kinetics can be tested by correct answers- UV-Vis spectroscopy - Fluorescence - FRET Modes of inhibition correct answers UV-Vis spectroscopy correct answers- light absorption by chromophores - measure the amount of l...

Test Bank for Biochemistry, 10th Edition by Jeremy Berg, Gregory Gatto Jr.; Justin Hines; John L. Tymoczko; Lubert Stryer. Full Chapters test bank are included - Chapter 1 to 32 1 Biochemistry in Space and Time   2 Protein Composition and Structure   3 Binding and Molecular Recognition   4 Protein Methods  5 Enzymes: Core Concepts and Kinetics   6 Enzyme Catalytic Strategies   7 Enzyme Regulatory Strategies   8 DNA, RNA, and the Flow of Genetic Informa...

Enzymes that can bind only one substrate and catalyze one reaction exhibit which type of binding specificity? correct answer: Absolute binding The rate of an enzymatic reaction will ___________________ for every 10 degrees C temperature increase until the enzyme denatures. correct answer: Double All of the following conditions may result in a rise in CKBB levels except. a. Child birth b Spinal chord injury c. Myocardial infarction d. Brain tumor correct answer: c. Myocardial infarct...

Background: In this module, Enzyme assays and kinetics were studied to understand the catalytic efficiency of binding of enzymes. Enzymes are biomolecules that act as catalysts in organisms to bring about specific biochemical reactions. As catalysts, enzymes do not act directly in the reaction, but perform necessary actions that bring about the reaction. This is often accomplished by causing conformational changes in biomolecules via influence on intermolecular forces (Hbonding, van der Waa...

An α-helical arrangement of amino acids is considered to be what level of protein structure? correct answer: Secondary structure of the protein β- sheets and α-helices are examples of secondary structures. How these structures interact would be an example of tertiary structure. If a mutation is made within the active site of an enzyme resulting in a decrease in Km, which of the following will be true with respect to the enzyme kinetics? correct answer: The enzyme will require a lower ...

Pre-PCOA Exam Latest Update (2022/2023) Already Passed Methods to enhance a drug's solubility in a solvent 1. Heat 2. Co-solvents increase the solubility of hydrophobic molecules by reducing the dielectric constant of the solvent 3. pH-Assisted solubility processes of drug elimination from the body liver, kidney and bile primary, secondary, tertiary and quaternary structures of proteins a. 1° primary - amino acid sequence of the polypeptide (Controls levels 2, 3, and 4) b. 2° secondary - l...

Biochem Questions and Answers with Verified Solutions What is the primary structure of a protein? The primary structure of a protein is the linear sequence of amino acids. How do competitive inhibitors affect enzyme activity? Competitive inhibitors decrease enzyme activity by binding to the active site, preventing substrate binding. What is the function of chaperone proteins? Chaperone proteins assist in the proper folding of other proteins. What is the role of glycogen in the body? Gl...

A complex organic molecule that is necessary for enzyme function but is NOT permanently associated with the enzyme is a: A) prosthetic group. B) cofactor. C) holofactor. D) coenzyme. E) metal ion. - D) coenzyme. A double-reciprocal plot of 1/V0 versus 1/[S] for an enzyme in the presence of increasing concentrations of an uncompetitive inhibitor will have lines corresponding to the different inhibitor concentrations that are BEST described by which statement? A) The lines will intersect...

TABLE OF CONTENTS_ Part I The Molecular D esign of Life SECTION 1 Biochemistry Helps Us to Understand Our World Chapter 1 Biochemistry and the Unity of Life Chapter 2 Water, Weak Bonds, and the Generation of Order Out of Chaos SECTION 2 Protein Composition and Structure Chapter 3 Amino Acids Chapter 4 Protein Three-Dimensional Structure Chapter 5 Techniques in Protein Biochemistry SECTION 3 Basic Concepts and Kinetics of Enzymes Chapter 6 Basic Concepts of Enzyme Action Chapter 7 Kinetics and Re...