Structure and Function of Macromolecules
... just a few small monomers, by varying number, sequence and bonding arrangements. Our biological macromolecules are grouped into four categories: proteins, nucleic acids, lipids and carbohydrates. We shall discuss structure and functions of each group. Most of our biological molecules are assembled o ...
... just a few small monomers, by varying number, sequence and bonding arrangements. Our biological macromolecules are grouped into four categories: proteins, nucleic acids, lipids and carbohydrates. We shall discuss structure and functions of each group. Most of our biological molecules are assembled o ...
BIOCHEMISTRY NOTES
... E. Ways that cells regulate the rates of its reactions: 1. by regulating the concentrations of enzyme molecules, substrate molecules, and cofactor molecules 2. some enzymes are produced only when they are needed 3. some enzymes are produced in an inactive form, & must activated before they can be us ...
... E. Ways that cells regulate the rates of its reactions: 1. by regulating the concentrations of enzyme molecules, substrate molecules, and cofactor molecules 2. some enzymes are produced only when they are needed 3. some enzymes are produced in an inactive form, & must activated before they can be us ...
A Database of Peak Annotations of Empirically Derived Mass Spectra
... available. These can be used singly or in a concatenated fashion; together they contain the sequences of more than 12 million proteins. We have imported these into the Illinois Bio-Grid Mass Spectrometry Proteomics Database (IBG-MSP) along with annotations. The aim is to consolidate these now scatte ...
... available. These can be used singly or in a concatenated fashion; together they contain the sequences of more than 12 million proteins. We have imported these into the Illinois Bio-Grid Mass Spectrometry Proteomics Database (IBG-MSP) along with annotations. The aim is to consolidate these now scatte ...
9 Proteins Chapter 9 Proteins
... • Proteins are too large to pass through cell membranes, and are contained within the cells where they were formed unless the cell is damaged by disease or trauma. ...
... • Proteins are too large to pass through cell membranes, and are contained within the cells where they were formed unless the cell is damaged by disease or trauma. ...
LS1a Fall 09
... o Step 1: The incoming aminoacyl-tRNA binds to the A-site. o Step 2: The bond between the C-terminus of the amino acid chain and the tRNA in the P-site is broken as the amino acid chain makes a new bond to the amino-group of the amino acid in the A-site. The mRNA advances by three nucleotides, placi ...
... o Step 1: The incoming aminoacyl-tRNA binds to the A-site. o Step 2: The bond between the C-terminus of the amino acid chain and the tRNA in the P-site is broken as the amino acid chain makes a new bond to the amino-group of the amino acid in the A-site. The mRNA advances by three nucleotides, placi ...
Chapter 25
... • Organic molecules that exist in minute quantities in food – Essential vitamins must be obtained by diet ...
... • Organic molecules that exist in minute quantities in food – Essential vitamins must be obtained by diet ...
Juxtaposition of particular amino acid residues may contribute to the
... are often found in close proximity to residues of tyrosine. This relationship is readily discernible in three-dimensional representations of such proteins, and also occasionally, as in the disulphide knot system of fibrinogen, and in kringle structures, directly from primary structures. Extracellula ...
... are often found in close proximity to residues of tyrosine. This relationship is readily discernible in three-dimensional representations of such proteins, and also occasionally, as in the disulphide knot system of fibrinogen, and in kringle structures, directly from primary structures. Extracellula ...
Translation Notes 2015 - Liberty Union High School District
... process of converting mRNA into proteins. Takes place on a ribosome in the cytoplasm. The cytoplasm contains amino acids, tRNA, and ribosomes, which are all needed for protein synthesis. ...
... process of converting mRNA into proteins. Takes place on a ribosome in the cytoplasm. The cytoplasm contains amino acids, tRNA, and ribosomes, which are all needed for protein synthesis. ...
CS273_StructurePrediction3
... Protein Side-Chain Packing • Problem: given the backbone coordinates of a protein, predict the coordinates of the side-chain atoms ...
... Protein Side-Chain Packing • Problem: given the backbone coordinates of a protein, predict the coordinates of the side-chain atoms ...
Influenza A H3N2 (A/Perth/16/2009) Hemagglutinin / HA
... < 1.0 EU per μg protein as determined by the LAL method. ...
... < 1.0 EU per μg protein as determined by the LAL method. ...
Protein Folding in Silico. Woodhead Publishing Series in Biomedicine Brochure
... Brochure More information from http://www.researchandmarkets.com/reports/2719894/ ...
... Brochure More information from http://www.researchandmarkets.com/reports/2719894/ ...
Curtis, MD and Grossniklaus, U. (2003) A gateway cloning vector set
... as query against the amino acid sequence database through BLASTP 2.2.31+ at the National Center for Biotechnology Information website (www.ncbi.nlm.nih.giv/, Altschul, et al. 1997, Altschul et al. 2005). Protein domain searches were carried out against the Pfam protein families database (Finn et al. ...
... as query against the amino acid sequence database through BLASTP 2.2.31+ at the National Center for Biotechnology Information website (www.ncbi.nlm.nih.giv/, Altschul, et al. 1997, Altschul et al. 2005). Protein domain searches were carried out against the Pfam protein families database (Finn et al. ...
Slide 1
... This group includes several ligands that have found widespread popularity; e.g., lectins such as concanavalin (Con A) and lentil for glycoproteins; protein A and protein G for antibody; calmodulin for calcium-dependent enzymes; etc. ...
... This group includes several ligands that have found widespread popularity; e.g., lectins such as concanavalin (Con A) and lentil for glycoproteins; protein A and protein G for antibody; calmodulin for calcium-dependent enzymes; etc. ...
Chapter 20: Carboxylic Acids and Nitriles
... Proteins – Amides from Amino Acids Amino acids contain a basic amino group and an acidic carboxyl group Joined as amides between the NH2 of one amino acid and the CO2H to the next amino acid Chains with fewer than 50 units are called peptides Protein: large chains that have structural or ca ...
... Proteins – Amides from Amino Acids Amino acids contain a basic amino group and an acidic carboxyl group Joined as amides between the NH2 of one amino acid and the CO2H to the next amino acid Chains with fewer than 50 units are called peptides Protein: large chains that have structural or ca ...
Molecules of Life
... of carbon, hydrogen, and oxygen in a ratio of about one carbon to two hydrogen atoms to one oxygen atom. • Carbohydrates are a source of energy and are used as structural materials in organisms. ...
... of carbon, hydrogen, and oxygen in a ratio of about one carbon to two hydrogen atoms to one oxygen atom. • Carbohydrates are a source of energy and are used as structural materials in organisms. ...
Chapter 15: Amines 1. What are the different types of amines? Be
... amino acids depend on their side chains and how their ionic charges vary with pH.! 3.! Why do amino acids have “handedness”? Be able to explain what is responsible for handedness and recognize simple molecules that display this property. (not on exam)! 4.! What is the primary structure of a protein ...
... amino acids depend on their side chains and how their ionic charges vary with pH.! 3.! Why do amino acids have “handedness”? Be able to explain what is responsible for handedness and recognize simple molecules that display this property. (not on exam)! 4.! What is the primary structure of a protein ...
Non-natural amino acid
... Only 20 amino acids are used in the biosynthesis of proteins no fundamental reason other amino acids cannot be used in proteins ...
... Only 20 amino acids are used in the biosynthesis of proteins no fundamental reason other amino acids cannot be used in proteins ...
Yr12Ch12 - ChemistryVCE
... When the body digests food and absorbs glucose, the glucose is transported by the blood to the liver where it is converted to glycogen, a storage polysaccharide. The glycogen is slowly hydrolysed between meals to maintain a fairly constant concentration of glucose in the blood for use by tissues suc ...
... When the body digests food and absorbs glucose, the glucose is transported by the blood to the liver where it is converted to glycogen, a storage polysaccharide. The glycogen is slowly hydrolysed between meals to maintain a fairly constant concentration of glucose in the blood for use by tissues suc ...
Chapter 12 Pathways to biomolecules
... When the body digests food and absorbs glucose, the glucose is transported by the blood to the liver where it is converted to glycogen, a storage polysaccharide. The glycogen is slowly hydrolysed between meals to maintain a fairly constant concentration of glucose in the blood for use by tissues suc ...
... When the body digests food and absorbs glucose, the glucose is transported by the blood to the liver where it is converted to glycogen, a storage polysaccharide. The glycogen is slowly hydrolysed between meals to maintain a fairly constant concentration of glucose in the blood for use by tissues suc ...
Proteolysis
Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.