 
									
								
									1 - From protein structure to biological function through interactomics
									
... parallel recombinant protein expression and purification of the interacting partners; 3) physical-chemical characterization of the interactions and 4) identification and structural characterization of binding sites. The integrative nature of the approach allowed a better understanding of the works o ...
                        	... parallel recombinant protein expression and purification of the interacting partners; 3) physical-chemical characterization of the interactions and 4) identification and structural characterization of binding sites. The integrative nature of the approach allowed a better understanding of the works o ...
									Old exams 1. Which one of these answers best describes a
									
... 12.“Zinc Fingers” motifs are important in cellular regulation because they are? 13.A protein is most likely to have the highest proportion of which of the following amino acid residues buried within its core? ( Look at table at the back of test) 14.Which of the following increases membrane fluidity? ...
                        	... 12.“Zinc Fingers” motifs are important in cellular regulation because they are? 13.A protein is most likely to have the highest proportion of which of the following amino acid residues buried within its core? ( Look at table at the back of test) 14.Which of the following increases membrane fluidity? ...
									Ch. 5 Organic Chem
									
... chains aggregated into one macromolecule – collagen (connective tissue) – hemoglobin ...
                        	... chains aggregated into one macromolecule – collagen (connective tissue) – hemoglobin ...
									Practice Exam 1 Answers
									
... D. None of the above E. All of the above 7. The configuration of most α-carbon atoms of amino acids linked in a peptide bond is A. cis B. circular C. parallel D. trans E. perpendicular 8. If a particular reaction has a negative G, is it likely to occur? A. Not unless energy is added to the system. ...
                        	... D. None of the above E. All of the above 7. The configuration of most α-carbon atoms of amino acids linked in a peptide bond is A. cis B. circular C. parallel D. trans E. perpendicular 8. If a particular reaction has a negative G, is it likely to occur? A. Not unless energy is added to the system. ...
									Structure of proteins Insulin:
									
... collagen secretion forms its primary structure. When it is formed by 3 polypeptide chains the helix is called tropo- collagen. According to the 3 polypeptides we have five tybes of collagen depending on amino acids sequences. Type II, III and IV have similar amino acids sequence in their 3 polypepti ...
                        	... collagen secretion forms its primary structure. When it is formed by 3 polypeptide chains the helix is called tropo- collagen. According to the 3 polypeptides we have five tybes of collagen depending on amino acids sequences. Type II, III and IV have similar amino acids sequence in their 3 polypepti ...
									Review Sheet Exam 1 C483 Spring 2014
									
... Topics to knowReaction rates Thermodynamics Equilibrium Constants Activation Energy The scale of cell components (pp 24 and 25) Chapter 2- Water- This chapter should also have been substantially review. It covers the basic forces associated with water-water association, the dissolution of solutes in ...
                        	... Topics to knowReaction rates Thermodynamics Equilibrium Constants Activation Energy The scale of cell components (pp 24 and 25) Chapter 2- Water- This chapter should also have been substantially review. It covers the basic forces associated with water-water association, the dissolution of solutes in ...
									Protein purification: the basics
									
... Lowry assay (Cu reduction) The first step is a Biuret reaction which reduces Cu+2 to Cu+1 The second reaction uses Cu+1 to reduce the Folin-Ciocalteu reagent (phosphomolybdate and phosphotungstate). This is detectable in the range of 500 to 750 nm ...
                        	... Lowry assay (Cu reduction) The first step is a Biuret reaction which reduces Cu+2 to Cu+1 The second reaction uses Cu+1 to reduce the Folin-Ciocalteu reagent (phosphomolybdate and phosphotungstate). This is detectable in the range of 500 to 750 nm ...
									Biology 3 Study Guide – Exam #1
									
... general roles, structures of nucleic acids (DNA, RNA) nucleotide structure basic structure of double-stranded DNA ...
                        	... general roles, structures of nucleic acids (DNA, RNA) nucleotide structure basic structure of double-stranded DNA ...
									Unit 1 PPT 2 (2bi-ii Protein structure)
									
... • Occur between non-polar R groups along the length of the polypeptide. • Folding of these regions occurs so that they form a central hydrophobic core, separating non-polar hydrophobic R groups from aqueous solution while the polar hydrophilic R groups are expressed on the outside of the structure, ...
                        	... • Occur between non-polar R groups along the length of the polypeptide. • Folding of these regions occurs so that they form a central hydrophobic core, separating non-polar hydrophobic R groups from aqueous solution while the polar hydrophilic R groups are expressed on the outside of the structure, ...
									Biomolecule
									
... nucleic acids are called macromolecules because of their large size  The largest macromolecules are polymers because they are constructed of many subunits called monomers ...
                        	... nucleic acids are called macromolecules because of their large size  The largest macromolecules are polymers because they are constructed of many subunits called monomers ...
									Lecture on PROTEIN FOLDING
									
... Proteins loose their 3-D shape (denature) when the weak bonds that hold together the structure are broken. Weak bonds are broken when the temperature is raised from body temp (37 C) to about 60 C Or by changing the pH Or by using chemical agents ...
                        	... Proteins loose their 3-D shape (denature) when the weak bonds that hold together the structure are broken. Weak bonds are broken when the temperature is raised from body temp (37 C) to about 60 C Or by changing the pH Or by using chemical agents ...
									Compartimentation, biological membranes
									
... Modification of proteins in the Golgi apparatus: - alteration of amino acid side chains ...
                        	... Modification of proteins in the Golgi apparatus: - alteration of amino acid side chains ...
									C454_lect10 - University of Wisconsin
									
... The arginine is hydrolyzed to produce the urea and to reform the ornithine. The ornithine reenters the mitochondrial matrix. ...
                        	... The arginine is hydrolyzed to produce the urea and to reform the ornithine. The ornithine reenters the mitochondrial matrix. ...
									Bio301 Biochemistry I
									
... Where ci is the molar concentration of the ith ionic species and Zi is its ionic charge. At high ionic strengths the solubilities ofproteins as well as those of most other substances, decrease. This effect is known as salting out. You have given 1.0 M solutions of NaCl, (NH4) 2SO4 and K3PO4.In which ...
                        	... Where ci is the molar concentration of the ith ionic species and Zi is its ionic charge. At high ionic strengths the solubilities ofproteins as well as those of most other substances, decrease. This effect is known as salting out. You have given 1.0 M solutions of NaCl, (NH4) 2SO4 and K3PO4.In which ...
									The Chemistry of the cell
									
... helped and guided in the folding process by chaperone proteins • Many proteins have sugars, phosphate groups, fatty acids, and other molecules covalently attached to certain amino acids. Most of this is done in the endoplasmic reticulum. • Many proteins are targeted to specific organelles within the ...
                        	... helped and guided in the folding process by chaperone proteins • Many proteins have sugars, phosphate groups, fatty acids, and other molecules covalently attached to certain amino acids. Most of this is done in the endoplasmic reticulum. • Many proteins are targeted to specific organelles within the ...
									Cut and Paste Macromolecule Instructions
									
... 3. Where in a cell would long-chain carbohydrates be synthesized, and by what organelle? During what cellular process would this occur? 4. How does putting a double bond in the carbon chain of a lipid affect the structure of the fatty acid? 5. Based on what you have observed about lipid structure, c ...
                        	... 3. Where in a cell would long-chain carbohydrates be synthesized, and by what organelle? During what cellular process would this occur? 4. How does putting a double bond in the carbon chain of a lipid affect the structure of the fatty acid? 5. Based on what you have observed about lipid structure, c ...
									Beta sheets are twisted
									
... loop regions connecting alpha-helical segments can have important functions e.g. EF-hand and DNA-binding EF hand loop ~ 12 residues polar and hydrophobic a.a. conserved positions Glycine is invariant at the sixth position The calcium ion is octahedrally coordinated by carboxyl side chains, main chai ...
                        	... loop regions connecting alpha-helical segments can have important functions e.g. EF-hand and DNA-binding EF hand loop ~ 12 residues polar and hydrophobic a.a. conserved positions Glycine is invariant at the sixth position The calcium ion is octahedrally coordinated by carboxyl side chains, main chai ...
									Amino acids and protein (lect 3%2c 2015)
									
... α-carboxyl group of one amino acid (with side chain R1) forms a covalent peptide bond with α-amino group of another amino acid (with the side chain R2) by removal of a molecule of water. The result is : Dipeptide ( i.e. Two amino acids linked by one peptide bond). By the same way, the dipeptide can ...
                        	... α-carboxyl group of one amino acid (with side chain R1) forms a covalent peptide bond with α-amino group of another amino acid (with the side chain R2) by removal of a molecule of water. The result is : Dipeptide ( i.e. Two amino acids linked by one peptide bond). By the same way, the dipeptide can ...
									Biology 12 - Biologically Important Molecules – Review Worksheet
									
... to permanently change the 3 dimensional structure of a protein the subunit that makes up nucleic acids - 4 types in DNA are A C G T the smallest unit of matter that cannot normally be broken into smaller particles the process of breaking down large fat droplets into smaller fat droplets the loose as ...
                        	... to permanently change the 3 dimensional structure of a protein the subunit that makes up nucleic acids - 4 types in DNA are A C G T the smallest unit of matter that cannot normally be broken into smaller particles the process of breaking down large fat droplets into smaller fat droplets the loose as ...
									Cell organelles and functions
									
...  Nucleoplasm is a gel like substance that contains large quantities of DNA, which forms the gene.  One or more nucleoli are present in each nucleus.  The nucleolus synthesizes ribosomes, which inturn build proteins. ...
                        	...  Nucleoplasm is a gel like substance that contains large quantities of DNA, which forms the gene.  One or more nucleoli are present in each nucleus.  The nucleolus synthesizes ribosomes, which inturn build proteins. ...
									Biochemistry PPT - Madison County Schools
									
... Where fats have a third fatty acid linked to glycerol, phospholipids have a negatively charged phosphate group. This makes the “head” of the phospholipid hydrophilic; the hydrocarbon “tails” are hydrophobic. Phospholipids are the major components of cell membranes. In a cell membrane, the hydrophobi ...
                        	... Where fats have a third fatty acid linked to glycerol, phospholipids have a negatively charged phosphate group. This makes the “head” of the phospholipid hydrophilic; the hydrocarbon “tails” are hydrophobic. Phospholipids are the major components of cell membranes. In a cell membrane, the hydrophobi ...
									Organic Compounds
									
... down and replaced. Composed of Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur Provide structure for: cells, bones, muscles, tissues, organs, hormones…most everything in the body! ...
                        	... down and replaced. Composed of Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur Provide structure for: cells, bones, muscles, tissues, organs, hormones…most everything in the body! ...
									Organic Compounds PowerPoint PDF
									
... down and replaced. Composed of Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur Provide structure for: cells, bones, muscles, tissues, organs, hormones…most everything in the body! Special Function: Proteins are responsible for cell metabolism (via enzymes) ...
                        	... down and replaced. Composed of Carbon, Hydrogen, Oxygen, Nitrogen, and Sulfur Provide structure for: cells, bones, muscles, tissues, organs, hormones…most everything in the body! Special Function: Proteins are responsible for cell metabolism (via enzymes) ...
									Characteristics all organisms share
									
... simple and complex carbohydrates? Name and give an example of each ...
                        	... simple and complex carbohydrates? Name and give an example of each ...
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.
 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									 
									