F2 og F3. Protein struktur og analyse og Protein struktur og funktion Flashcards
Describe a competetive inhibitor that directly blocks substrate binding to an enzyme
Give a few examples of some general functions
Describe why A helix is a common, regular, biological structure
Describe why a protein is made of amino acids linked togehter into a polypeptide chain
Make a schematic model of how a motor protein uses ATP hydrolysis to move in one direction along a cytoskeletal filament
Desciribe a series of enzyme-catalyzed reactions forms a linked pathway
Explain how a single type of protein subunit can pack together to form a filament, a hollow tube, or a spherical shell
Make a survey of nucleotides
Explain acids
Show how affinity chromatography can be used to isolate the binding partners of a protein of interest
Show how all amino acids have an amino group, a carboxyl group, and a side chain (R) attached to their a-carbon atom
Draw alpha and beta links
Show alternating double bonds
Show how amino acids are linked together by peptide bonds
Show how Amino acids in a protein are held together by peptide bonds
Show how An actin filament is composed of identical protein subunits
Show how an antibody is Y-shaped and ahs two identical antigen-binding sites, one on each arm of the Y
Show how an energetically unfavorable reaction can be driven by an energetically favorable follow on reaction that acts as a chemical siphon
show how An enzyme’s performance depends on how rapidly it can process its substrate
Explain bases
Show how beta sheets can stack to form an amyloid structure
Show how beta sheets come in two varieties
show how Binding sites allow proteins to interact with specific ligands
Breaking open cells and tissues
show how carbon atoms cycle continuously through the biosphere
Draw carbon skeletons
Show how catabolic and anabolic pathways together constitue the cell’s metabolism
Draw C-H compunds
Explain how changes in conformation can allow a protein to walk along a cytoskeletal filament
Show how chaperone proteins can guide the folding of a newly synthesized polypeptide chai
Draw C-N compounds
Draw C-O compounds
Draw complex oligosaccharides
Explain covavlent bonds
Show how Denatured proteins can often recover their natural shapes
Draw di-, oligo- and polysaccharides
Explain how Disulfide bonds help stabilize a favored protein conformation
Explain electrostatic attraction in water.
Draw electrostatic attractio
Explain why Energetically favorable reactions have a negative DeltaG, whereas energetically unfavorable reactions have a positive DeltaG
Show how enzymes bind to, and chemically alter, substrate molecuels
Show how Enzymes can encourage a reaction in several ways
Show how enzymes catalyze reactions by lowering the activation-energy barrier
Show how enzymes convert substrates to products while remaining unchanged themselves
Howcome even energetically favorable reactions require activation energy to get them started
Explain fatty acids
Explain how Feedback inhibition at multiple points regulates connected metabolic pathways
Explain how Feedback inhibition regulates the fow through biosynthetic pathways
Explain how Feedback inhibition triggers a conformational change in an enzyme
Describe how Fibrous proteins collagen and elastin form very different structures
Explain Free energy
Make an overview over historical landmarks in our understanding of proteins
Draw hydrogen bonds in water.
Explain how Hydrogen bonds within a protein molecule help stabilize its folded shape
Draw hydrogen bonds
Draw a hydrogen ion exchange
Draw hydrophilic molecules
Show how hydrophobic forces help proteins fold into compact conformations
Explain hydrophobic forces
Draw hydrophobic molecules
Explain how Identical protein subunits can assemble into complex structures
Explain how Intertwined alpha helices can form a still coiled-coil
Explain how intracellular condensates can form biochemical subcompartments in cells
Draw isomers
Explain how living cells do not defy the second law of thermodynamics
Explain how lowering the activation energy greatly increases the probability that a reaction will occur.
Explain how Lysozyme cleaves a polysaccharide chain
Explain how many different GTP- binding proteins function as molecular switches
Explain how Many protein molecules contain multiple copes of the same protein subunit
Explain how Many proteins are composed of separate functional domain
Explain how Many viral capsids are essentially spherical protein assemblies
Explain how Mass spectrometry can be used to identify proteins by determining the precise masses of peptides derived from them
Explain how Measured reaction rates plotted to determine the Vmax and Km of an enzyme-catalyzed reaction
Draw monosaccharides
Explain how Most proteins belong structurally related families
Explain how oxidation and reduction involve a shift in the balance of electrons
Explain pH.
Explain phosphates
Explain how photosynthesis and cell respiration are complementary processes in the living world
Explain how Prion diseases are caused by proteins whose misfolding is infectious.
Explain how Protein conformation can be represented in a variety of ways
Explain how Protein machines can carry out complex functions
Explain how Protein phosphorylation is a very common mechanism for regulating protein activity.
Explain Protein separation by chromatrography
Explain how Reaction coupling can drive an energetically unfavorable reaction
Explain how Reactions will eventually reach a chemical equlibrium
Explain how Retinal and heme are required for the function of certain proteins
Explain how Ribbon models show these different protein domains
Draw ring formation
Explain how Scaffold proteins can concentrate interacting proteins in the cel
Explain how Serine proteases constitute a family of proteolytic enzymes
Explain how small changes in the number of weak bonds can have drastic effects on a binding interaction
Explain how some chaperone proteins act as isolation chambers that help a polypeptide fold
List some common functional classes of enzymes
Explain how some polypeptide chains fold into an orderly pattern called a beta sheet
Explain how Some polypeptide chains fold into an orderly repeating form known as an alpha helix
Explain how Some proteins are formed as a symmetrical assembly of two different subunits
Explain how Spherical, liquid-drop-like nucleoli can be seen to fuse in the light microscope
Draw sugar derivatives
Draw sulfhydryl groups
Explain the amino acids found in proteins
Explain the antibody molecule
Explain why the binding of a protein to another molecule is highly selective
Explain how The binding of a regulatory ligand can change the eqilibrium between two protein conformations
Explain why The equilibrium constant, K, for the reaction A+B —> AB depends on the concentrations of A, B and AB
Explain how The modification of a protein at multiple sites can control the protein’s behavior
Explain how three types of noncovalent bonds help proteins fold
Explain the Twenty different amino acids are commonly found in proteins
Explain van der waals attractions
Explain water as a solvent
Draw and explain water.
Explain weak noncovalent chemical bonds
Explain x-ray crystallography
