Bio Inorganic Chemistry
... •Cooperativity: The phenomenon that binding of an effector molecule to a biological system either enhances or diminishes the binding of successive molecules, e.g. hemoglobin Corrin: Ring‐contracted porphyrinderivative that is missing a carbon Cytochrome: Hemeprotein that transfers electrons, an ...
... •Cooperativity: The phenomenon that binding of an effector molecule to a biological system either enhances or diminishes the binding of successive molecules, e.g. hemoglobin Corrin: Ring‐contracted porphyrinderivative that is missing a carbon Cytochrome: Hemeprotein that transfers electrons, an ...
Amino acid side chains stabilise the enzyme shape Hydrogen bonds
... Many amino acids contain groups in the side chains that have a hydrogen atom attached to either an oxygen or nitrogen atom. Hydrogen bonding can occur between such groups. ...
... Many amino acids contain groups in the side chains that have a hydrogen atom attached to either an oxygen or nitrogen atom. Hydrogen bonding can occur between such groups. ...
Formula Notes and Criss Cross Method
... Written below and after the symbol of the atom to indicate the number of atoms of that element in the compound. if no subscript, then = 1 atom Example: H2O ...
... Written below and after the symbol of the atom to indicate the number of atoms of that element in the compound. if no subscript, then = 1 atom Example: H2O ...
Polyatomic Ions (Memorize for Wednesday, January 31
... EX – H2SO4: sulfate ion changes to sulfuric acid Polyatomic ions ending in –ite form acids with an –ous ending EX – HClO2: chlorite ion changes to chlorous acid The number of hydrogen atoms equals the charge on the polyatomic ion EX – H3PO4: H+1 x 3 = PO4-3 ...
... EX – H2SO4: sulfate ion changes to sulfuric acid Polyatomic ions ending in –ite form acids with an –ous ending EX – HClO2: chlorite ion changes to chlorous acid The number of hydrogen atoms equals the charge on the polyatomic ion EX – H3PO4: H+1 x 3 = PO4-3 ...
Serine Proteases Teaching Exercises
... c. Find phenylalanine, tyrosine, tryptophan and methionine. 4. When these enzymes are made, they are initially in an inactive precursor state, called zymogens. In order for the enzymes to become active, they will be cleaved to arrange the linear amino acid sequence in such a fashion as to orient thr ...
... c. Find phenylalanine, tyrosine, tryptophan and methionine. 4. When these enzymes are made, they are initially in an inactive precursor state, called zymogens. In order for the enzymes to become active, they will be cleaved to arrange the linear amino acid sequence in such a fashion as to orient thr ...
Measurement of Protein Molecular Weight using MALDI MS
... To calculate the molecular weight of the protein, the measured m/z value of charge state, n, is multiplied by n and then n protons (n * 1.0079) are subtracted to give the measured molecular weight. ...
... To calculate the molecular weight of the protein, the measured m/z value of charge state, n, is multiplied by n and then n protons (n * 1.0079) are subtracted to give the measured molecular weight. ...
Coordination Compounds
... • Complex ion: can be cation or anion; contains the transition metal and usually is in brackets. • Ligands: neutral molecule or ion having a lone pair of electrons that forms a coordinate covalent bond to a metal ion; usually dissociate when aqueous. Ligands in the spectrochemical series show which ...
... • Complex ion: can be cation or anion; contains the transition metal and usually is in brackets. • Ligands: neutral molecule or ion having a lone pair of electrons that forms a coordinate covalent bond to a metal ion; usually dissociate when aqueous. Ligands in the spectrochemical series show which ...
Lesson
... * Amino acid structure & properties * Stages involved with formation of proteins * Primary, secondary, tertiary & quaternary structures ...
... * Amino acid structure & properties * Stages involved with formation of proteins * Primary, secondary, tertiary & quaternary structures ...
this lecture as PDF here
... Enzymes require an additional non-protein component to carry out its catalytic functions. ...
... Enzymes require an additional non-protein component to carry out its catalytic functions. ...
Protein Engineering
... •Increase the efficiency of enzyme-catalyzed reactions • Eliminate the need for cofactor in enzymatic reaction •Change substrate binding site to increase specificity •Change the thermal tolerance •Change the pH stability •Increase proteins resistance to proteases (purification) •Signal sequences - s ...
... •Increase the efficiency of enzyme-catalyzed reactions • Eliminate the need for cofactor in enzymatic reaction •Change substrate binding site to increase specificity •Change the thermal tolerance •Change the pH stability •Increase proteins resistance to proteases (purification) •Signal sequences - s ...
Unidentate, Bidentate and Multidentate Ligands
... In the examples we've already looked at, each ligand only forms one bond with the central metal ion to give the complex ion. Such a ligand is said to be unidentate. That means literally that it only has one tooth! It only has one pair of electrons that it can use to bond to the metal - any other lon ...
... In the examples we've already looked at, each ligand only forms one bond with the central metal ion to give the complex ion. Such a ligand is said to be unidentate. That means literally that it only has one tooth! It only has one pair of electrons that it can use to bond to the metal - any other lon ...
The World of Chemistry
... 1. What are some of the ways mentioned that proteins are used in our bodies? ...
... 1. What are some of the ways mentioned that proteins are used in our bodies? ...
BIO 6.3 Carbon - Steinbach Science
... because amino acids can be put in various combinations The number of amino acids in protein chains determine the kind of protein Proteins are the building blocks of many structural components of orga ...
... because amino acids can be put in various combinations The number of amino acids in protein chains determine the kind of protein Proteins are the building blocks of many structural components of orga ...
Metalloprotein
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large number of all proteins are part of this category.
