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Hydrolysis and Dehydration Synthesis: How we become what we eat
... o Monosaccharides are simple sugars, i.e., glucose and fructose o Complex carbohydrates form when glucose bonds with another monosaccharide o Lipids o Triglycerides – 3 fatty acids + glyceride o Steroids – cholesterol and hormones o Protein o Made of amino acids o Enzymes speed up chemical reactions ...
... o Monosaccharides are simple sugars, i.e., glucose and fructose o Complex carbohydrates form when glucose bonds with another monosaccharide o Lipids o Triglycerides – 3 fatty acids + glyceride o Steroids – cholesterol and hormones o Protein o Made of amino acids o Enzymes speed up chemical reactions ...
No Slide Title
... z Proteins are single, unbranched chains of amino acid monomers z There are 20 different amino acids z A protein’s amino acid sequence determines its three-dimensional structure (conformation) z In turn, a protein’s structure determines the function of that protein ...
... z Proteins are single, unbranched chains of amino acid monomers z There are 20 different amino acids z A protein’s amino acid sequence determines its three-dimensional structure (conformation) z In turn, a protein’s structure determines the function of that protein ...
peptides
... Oligopeptide (peptide): a short chain of 20-30 amino acids Polypeptide: a longer peptide with no particular structure Protein: a polypeptide chains with an organized 3D structures The average molecular weight of an amino acid residue is about 110 The molecular weights of most proteins are between 55 ...
... Oligopeptide (peptide): a short chain of 20-30 amino acids Polypeptide: a longer peptide with no particular structure Protein: a polypeptide chains with an organized 3D structures The average molecular weight of an amino acid residue is about 110 The molecular weights of most proteins are between 55 ...
Four Levels of Protein Structure
... Four Levels of Protein Structure • Primary Structure: Linear Sequence of Amino Acids Each amino acid has central carbon liked to ---hydrogen (H) ---amino group (NH2) ...
... Four Levels of Protein Structure • Primary Structure: Linear Sequence of Amino Acids Each amino acid has central carbon liked to ---hydrogen (H) ---amino group (NH2) ...
Biochem SG06
... SC.F.1.4.5 The student knows that complex interactions among the different kinds of molecules in the cell cause distinct cycles of activity governed by proteins. DS 4.14 ...
... SC.F.1.4.5 The student knows that complex interactions among the different kinds of molecules in the cell cause distinct cycles of activity governed by proteins. DS 4.14 ...
USMLE Step 1 Web Prep — The Genetic Code, Mutations, and
... As proteins emerge from ribosomes, they fold into three-dimensional conformations that are essential for their subsequent biologic activity. Generally, four levels of protein shape are distinguished: 1. Primary--sequence of amino acids specified in the gene. 2. Secondary--folding of the amino acid c ...
... As proteins emerge from ribosomes, they fold into three-dimensional conformations that are essential for their subsequent biologic activity. Generally, four levels of protein shape are distinguished: 1. Primary--sequence of amino acids specified in the gene. 2. Secondary--folding of the amino acid c ...
Document
... Molecular surface of several proteins showing their comparative sizes. From left to right: Antibody (IgG), Hemoglobin, Insulin (a hormone), and Glutamine synthetase (an enzyme). ...
... Molecular surface of several proteins showing their comparative sizes. From left to right: Antibody (IgG), Hemoglobin, Insulin (a hormone), and Glutamine synthetase (an enzyme). ...
Amino Acid Alphabet
... losing its original hydrogen an amide nitrogen will pick up a deuterium The rate of exchange can be monitored by mass spec or by NMR green: no exchange blue: too fast red: just right H/D exchange can be used to : Measure the rate of folding and unfolding Solvent accessibility at protein-protein inte ...
... losing its original hydrogen an amide nitrogen will pick up a deuterium The rate of exchange can be monitored by mass spec or by NMR green: no exchange blue: too fast red: just right H/D exchange can be used to : Measure the rate of folding and unfolding Solvent accessibility at protein-protein inte ...
FlexWeb
... changes in dihedral angles of rotatable bonds. • Rigidity analysis, using the pebble game and FIRST, determines which dihedral angles are rotatable and which are locked. • The rigidity of the three-dimensional folded protein is determined by the constraints introduced by hydrogen bonds and hydrophob ...
... changes in dihedral angles of rotatable bonds. • Rigidity analysis, using the pebble game and FIRST, determines which dihedral angles are rotatable and which are locked. • The rigidity of the three-dimensional folded protein is determined by the constraints introduced by hydrogen bonds and hydrophob ...
Lecture 7 Proteins 1. Which amino acids are considered as acidic
... sulphate is the most commonly used salt as it is cheap and sufficiently soluble. Other salts which can be used are ammonium acetate, sodium sulphate, and sodium citrate. 6. How to differentiate between secondary and tertiary structure of proteins? Answer: Tertiary protein structure refers to the com ...
... sulphate is the most commonly used salt as it is cheap and sufficiently soluble. Other salts which can be used are ammonium acetate, sodium sulphate, and sodium citrate. 6. How to differentiate between secondary and tertiary structure of proteins? Answer: Tertiary protein structure refers to the com ...
... surface would be used, but the speed of rotation would have to be high so as not to form a simple spiral. At high speeds the protein would be held on the wall by centrifugal force but liquids entering at the top would not just pass down and out the tip but would rise up again when they reached the b ...
Chapter 5 – The Proteins and Amino Acids
... and repair of body tissue requires a continual supply of amino acids to synthesize proteins. Growth of new tissue requires additional protein. The Functions of Body Proteins The major role of dietary protein is to supply amino acids for the synthesis of proteins needed in the body, although dietary ...
... and repair of body tissue requires a continual supply of amino acids to synthesize proteins. Growth of new tissue requires additional protein. The Functions of Body Proteins The major role of dietary protein is to supply amino acids for the synthesis of proteins needed in the body, although dietary ...
Notes Chemical Basis for Life BIO.A.2
... absorb lots of heat energy without drastically changing its temperature • Water stays in a liquid phase over much of the planet and therefore supports life • Density of ice – allows ice to float • Most biological reactions require water. • More about water…. ...
... absorb lots of heat energy without drastically changing its temperature • Water stays in a liquid phase over much of the planet and therefore supports life • Density of ice – allows ice to float • Most biological reactions require water. • More about water…. ...
Protein Folding, Shape, and Function Activity Instructions
... A chart of the amino acid sidechains and their properties is available for reference. 5. In addition to using the principles above to fold your protein, also form a pocket or groove (representing an active site) around a small lego (representing the substrate). This active site and substrate should ...
... A chart of the amino acid sidechains and their properties is available for reference. 5. In addition to using the principles above to fold your protein, also form a pocket or groove (representing an active site) around a small lego (representing the substrate). This active site and substrate should ...
ppt file
... in the DIP (Database of Interacting Proteins). The September 1, 2002, update of the DIP data set containing 14,871 interactions for 4,692 proteins is used. By comparing the probabilities of associations for all possible protein pairs in the measured protein interaction network with those in the ot ...
... in the DIP (Database of Interacting Proteins). The September 1, 2002, update of the DIP data set containing 14,871 interactions for 4,692 proteins is used. By comparing the probabilities of associations for all possible protein pairs in the measured protein interaction network with those in the ot ...
Organic Notes.graffle
... What are their functions? This depends on the organism and location of the lipid, but generally, they are the major component of cell membranes, they area used for energy (often stored in fat cells). There are many functions in living things. The two above are enough to know for this course. ...
... What are their functions? This depends on the organism and location of the lipid, but generally, they are the major component of cell membranes, they area used for energy (often stored in fat cells). There are many functions in living things. The two above are enough to know for this course. ...
Supplementary Tables and Figures Legends (doc 39K)
... ciprofloxacin, daunorubicin, kanamycin and paroxetine used to identify frequent hitters in K562, KU812 and chronic phase CML patient cells. Amino groups employed to immobilize each drug on the Sepharose beads (Rix, 2007) are shown in blue. The five compounds, being drugs themselves, were chosen for ...
... ciprofloxacin, daunorubicin, kanamycin and paroxetine used to identify frequent hitters in K562, KU812 and chronic phase CML patient cells. Amino groups employed to immobilize each drug on the Sepharose beads (Rix, 2007) are shown in blue. The five compounds, being drugs themselves, were chosen for ...
Peptides
... Oligopeptide (peptide): a short chain of 20-30 amino acids Polypeptide: a longer peptide with no particular structure Protein: a polypeptide chains with an organized 3D structures The average molecular weight of an amino acid residue is about 110 The molecular weights of most proteins are between 55 ...
... Oligopeptide (peptide): a short chain of 20-30 amino acids Polypeptide: a longer peptide with no particular structure Protein: a polypeptide chains with an organized 3D structures The average molecular weight of an amino acid residue is about 110 The molecular weights of most proteins are between 55 ...
Biochemistry - Bishop Ireton High School
... • Amino group- NH2 • Carboxyl group-COOH • R group- R groups are different for each of the 20 amino acids. ...
... • Amino group- NH2 • Carboxyl group-COOH • R group- R groups are different for each of the 20 amino acids. ...
Molecules of Life Online Organizer
... Each enzyme catalyzes ______________ specific reaction. Enzymes are / are not changed in a chemical reaction. Circle the correct answer ...
... Each enzyme catalyzes ______________ specific reaction. Enzymes are / are not changed in a chemical reaction. Circle the correct answer ...
Lipids,proteins, and nucleic acids
... • Proteins contain many amino acids and are often amphiphilic • -R groups determine shape of protein ...
... • Proteins contain many amino acids and are often amphiphilic • -R groups determine shape of protein ...
Lipids,proteins, and nucleic acids
... • Proteins contain many amino acids and are often amphiphilic • -R groups determine shape of protein ...
... • Proteins contain many amino acids and are often amphiphilic • -R groups determine shape of protein ...
Cyclol
![](https://commons.wikimedia.org/wiki/Special:FilePath/Cyclol_reaction.png?width=300)
The cyclol hypothesis is the first structural model of a folded, globular protein. It was developed by Dorothy Wrinch in the late 1930s, and was based on three assumptions. Firstly, the hypothesis assumes that two peptide groups can be crosslinked by a cyclol reaction (Figure 1); these crosslinks are covalent analogs of non-covalent hydrogen bonds between peptide groups. These reactions have been observed in the ergopeptides and other compounds. Secondly, it assumes that, under some conditions, amino acids will naturally make the maximum possible number of cyclol crosslinks, resulting in cyclol molecules (Figure 2) and cyclol fabrics (Figure 3). These cyclol molecules and fabrics have never been observed. Finally, the hypothesis assumes that globular proteins have a tertiary structure corresponding to Platonic solids and semiregular polyhedra formed of cyclol fabrics with no free edges. Such ""closed cyclol"" molecules have not been observed either.Although later data demonstrated that this original model for the structure of globular proteins needed to be amended, several elements of the cyclol model were verified, such as the cyclol reaction itself and the hypothesis that hydrophobic interactions are chiefly responsible for protein folding. The cyclol hypothesis stimulated many scientists to research questions in protein structure and chemistry, and was a precursor of the more accurate models hypothesized for the DNA double helix and protein secondary structure. The proposal and testing of the cyclol model also provides an excellent illustration of empirical falsifiability acting as part of the scientific method.