Food Chemistry
... scituliceps showed high proteolytic activity and unwent auto-hydrolysis. The highest proteolytic activity was at 65 °C and its optimum pH was 7.5. When assayed in the presence of several protease inhibitors, the enzymes were completely inactivated by soybean trypsin inhibitor. The in vitro digestibi ...
... scituliceps showed high proteolytic activity and unwent auto-hydrolysis. The highest proteolytic activity was at 65 °C and its optimum pH was 7.5. When assayed in the presence of several protease inhibitors, the enzymes were completely inactivated by soybean trypsin inhibitor. The in vitro digestibi ...
AP Biology Study Guide
... Types of macromolecules, their structures, and functions: lipids, carbohydrates, nucleic acids, proteins Water and its unique properties Types of bonds Enzyme structure and function; different types of enzymes, factors that affect enzyme function Metabolism: catabolic vs. anabolic Atomic ...
... Types of macromolecules, their structures, and functions: lipids, carbohydrates, nucleic acids, proteins Water and its unique properties Types of bonds Enzyme structure and function; different types of enzymes, factors that affect enzyme function Metabolism: catabolic vs. anabolic Atomic ...
Chapter 2 Molecules to enzymes Short Answer
... e. transcription produces RNA sequence complementary to the DNA sequence (of the gene); f. triplets of nucleotides on mRNA are codons; g. translation converts mRNA sequence of information into a specific amino acid chain (polypeptide); h. (each class of) tRNA carries a specific triplet of (three) ba ...
... e. transcription produces RNA sequence complementary to the DNA sequence (of the gene); f. triplets of nucleotides on mRNA are codons; g. translation converts mRNA sequence of information into a specific amino acid chain (polypeptide); h. (each class of) tRNA carries a specific triplet of (three) ba ...
amino acids
... • Negatively charged amino acids are often found near the amino terminus of the helical segment, where they have a stabilizing interaction with the positive charge of the helix dipole. • A positively charged amino acid at the aminoterminal end is ...
... • Negatively charged amino acids are often found near the amino terminus of the helical segment, where they have a stabilizing interaction with the positive charge of the helix dipole. • A positively charged amino acid at the aminoterminal end is ...
The Concept of Functional Constraint
... Thus, a protein in which the active sites constitute only 1% of its sequence will be less constrained, and therefore will evolve more quickly than a protein that devotes 50% of its sequence to performing specific biochemical or physiological tasks. ...
... Thus, a protein in which the active sites constitute only 1% of its sequence will be less constrained, and therefore will evolve more quickly than a protein that devotes 50% of its sequence to performing specific biochemical or physiological tasks. ...
FARM ANIMAL NUTRITION
... • Structural components of cells and organs. • Sources of energy for maintenance & ...
... • Structural components of cells and organs. • Sources of energy for maintenance & ...
biol-1406_ch3.ppt
... • Amino acids are joined to form chains by dehydration synthesis – An amino group reacts with a carboxyl group, and water is lost ...
... • Amino acids are joined to form chains by dehydration synthesis – An amino group reacts with a carboxyl group, and water is lost ...
Red meat and protein
... Diets must provide the right balance of amino acids and nitrogen essential for the body to be able to synthesise protein for growth and maintenance. Protein quality is a measure of how well or poorly the body can use a given protein to meet its needs. This is dependent on the essential amino acid co ...
... Diets must provide the right balance of amino acids and nitrogen essential for the body to be able to synthesise protein for growth and maintenance. Protein quality is a measure of how well or poorly the body can use a given protein to meet its needs. This is dependent on the essential amino acid co ...
Power point presentation
... represents a functional group that varies depending on the specific amino acid in question. There are 20 amino acids. ...
... represents a functional group that varies depending on the specific amino acid in question. There are 20 amino acids. ...
Biochemistry PowerPoint 1
... compounds. • These reactive clusters of atoms are called functional groups. • Elements include: H, O, S & P ...
... compounds. • These reactive clusters of atoms are called functional groups. • Elements include: H, O, S & P ...
What are proteins?
... Compare the amino acids to each other. Circle in green the amino group (-NH2) of each amino acid. Circle in blue the carboxyl group (-COOH) of each amino acid. Circle in red the part of the amino acid that is different in every amino acid? Which parts of the amino acid are the same in every amino ac ...
... Compare the amino acids to each other. Circle in green the amino group (-NH2) of each amino acid. Circle in blue the carboxyl group (-COOH) of each amino acid. Circle in red the part of the amino acid that is different in every amino acid? Which parts of the amino acid are the same in every amino ac ...
Unit 3 Macromolecules, enzymes, and ATP
... Contributes to vital information and control processes in the body. It also functions as fundamental and structural substances for cells, cell walls, and the intracellular matrix Blood types- blood types A and B only differ from blood type O by the presence of an additional monosaccharide, N-acetylg ...
... Contributes to vital information and control processes in the body. It also functions as fundamental and structural substances for cells, cell walls, and the intracellular matrix Blood types- blood types A and B only differ from blood type O by the presence of an additional monosaccharide, N-acetylg ...
Polymer - Deans Community High School
... All proteins contain the elements C,N,O,H. They are condensation polymers, made by amino acids linking together. An amine group of one molecule links to the carboxyl group of another molecule to form an amide or peptide bond. The body makes specific proteins it needs, but cannot make all the amino a ...
... All proteins contain the elements C,N,O,H. They are condensation polymers, made by amino acids linking together. An amine group of one molecule links to the carboxyl group of another molecule to form an amide or peptide bond. The body makes specific proteins it needs, but cannot make all the amino a ...
HNF4a Network - University of Wisconsin–Madison
... • They verified binding at more than 50 randomly selected targets of HNF4a in hepatocytes by conventional genespecific ChIP. • When antibodies against HNF4a were used for ChIP in control experiments with Jurkat, U937, and BJT cells, no more than 17 promoters were identified. • When preimmune antibod ...
... • They verified binding at more than 50 randomly selected targets of HNF4a in hepatocytes by conventional genespecific ChIP. • When antibodies against HNF4a were used for ChIP in control experiments with Jurkat, U937, and BJT cells, no more than 17 promoters were identified. • When preimmune antibod ...
Bio251 07 HW2 1-26-0..
... Hydrophilic. The Oxygen atom attracts electrons much more forcefully than does a Hydrogen atom. In this way, oxygen is a strongly electronegative atom. As a result the O-H bond is said to be polarized, such that one of the atoms has a partial negative charge, and the other a partial positive charge. ...
... Hydrophilic. The Oxygen atom attracts electrons much more forcefully than does a Hydrogen atom. In this way, oxygen is a strongly electronegative atom. As a result the O-H bond is said to be polarized, such that one of the atoms has a partial negative charge, and the other a partial positive charge. ...
1-1 - Test Bank Exam
... fluorescent or luminescent molecule. Immunofluorescence (IF) provides a way to visualize a particular protein within a cell using microscopy: the cell is “fixed” (killed and preserved intact), flooded with an antibody that binds a protein of interest, and washed free of unbound antibody. Because the ...
... fluorescent or luminescent molecule. Immunofluorescence (IF) provides a way to visualize a particular protein within a cell using microscopy: the cell is “fixed” (killed and preserved intact), flooded with an antibody that binds a protein of interest, and washed free of unbound antibody. Because the ...
DNA Fill in the blank notes.
... called _______________ and ends at a place on DNA that is called a ___________ _____________. Protein Synthesis or Translation Once a strand of mRNA is made, and moves out of the nucleus, the process of making proteins can begin. This process is called ____________________. The process takes place ‘ ...
... called _______________ and ends at a place on DNA that is called a ___________ _____________. Protein Synthesis or Translation Once a strand of mRNA is made, and moves out of the nucleus, the process of making proteins can begin. This process is called ____________________. The process takes place ‘ ...
Gene Duplication in the Mo-Fe Protein of Nitrogenase
... some of them symbiotic with plants • catalyzes the conversion of molecular nitrogen (N2) from the air into ammonia (NH3). • It is found in a variety of bacteria, some of them symbiotic with plants. ...
... some of them symbiotic with plants • catalyzes the conversion of molecular nitrogen (N2) from the air into ammonia (NH3). • It is found in a variety of bacteria, some of them symbiotic with plants. ...
2.3 Carbon Compounds
... temperature Saturated fatty acids tend to be solid at room temperature. ...
... temperature Saturated fatty acids tend to be solid at room temperature. ...
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.