Chapter 21
... - These coils wind around other coils making larger and stronger structures (like hair). - α-helix chains bond together by disulfide bond (-S-S-) - More disulfide bonds, more rigid materials (horns & nails). ...
... - These coils wind around other coils making larger and stronger structures (like hair). - α-helix chains bond together by disulfide bond (-S-S-) - More disulfide bonds, more rigid materials (horns & nails). ...
Chapter 23 - Evangel University
... • The breakdown of carbon skeletons follows two pathways, depending on the type of end product • _________________ amino acid: one whose carbon skeleton is degraded to pyruvate or oxaloacetate, both of which may then be converted to glucose • _________________ amino acid: one whose carbon skeleton i ...
... • The breakdown of carbon skeletons follows two pathways, depending on the type of end product • _________________ amino acid: one whose carbon skeleton is degraded to pyruvate or oxaloacetate, both of which may then be converted to glucose • _________________ amino acid: one whose carbon skeleton i ...
Three-Point Binding Model
... Three-Point Binding Model • First proposed by Ogsten (1948) to explain biological enantioselection/enantiospecificity • Serves as a model for chromatographic chiral stationary phases Preferential binding occurs via intramolecular non-covalent forces: H-bonding salt bridge Ionic Dipole-dipole Van der ...
... Three-Point Binding Model • First proposed by Ogsten (1948) to explain biological enantioselection/enantiospecificity • Serves as a model for chromatographic chiral stationary phases Preferential binding occurs via intramolecular non-covalent forces: H-bonding salt bridge Ionic Dipole-dipole Van der ...
Chapter 7 - Coenzymes
... There are other groups that contribute to the reactivity of enzymes beside amino acid residues. These groups are called cofactors - chemicals required by apoenzymes (inactive) to become holoenzymes (active). There are two types of cofactors: 1) essential ions - metal ions -inorganic 2) coenzymes - o ...
... There are other groups that contribute to the reactivity of enzymes beside amino acid residues. These groups are called cofactors - chemicals required by apoenzymes (inactive) to become holoenzymes (active). There are two types of cofactors: 1) essential ions - metal ions -inorganic 2) coenzymes - o ...
Ecology Review Science Department
... and what does it do? A Biological catalyst that speeds up reactions by decreasing activation energy. ...
... and what does it do? A Biological catalyst that speeds up reactions by decreasing activation energy. ...
Microbiology bio 123
... weight (not as large as protein). If absent in a holoenzyme, the enzyme will not work and is then not called a holoenzyme. 3. Co-factor – required by some enzymes, typically a metallic ion; is inorganic. Approximate size of an enzyme: 10,000-1,000,000 amu (amu is equal to the weight of a proton, H2O ...
... weight (not as large as protein). If absent in a holoenzyme, the enzyme will not work and is then not called a holoenzyme. 3. Co-factor – required by some enzymes, typically a metallic ion; is inorganic. Approximate size of an enzyme: 10,000-1,000,000 amu (amu is equal to the weight of a proton, H2O ...
A. Primary structure: - B. Secondary structure: -
... 3. α – helix is stabilized by intrachain hydrogen bonds between C=O of each peptide bond and the NH of the peptide bond four residues away ...
... 3. α – helix is stabilized by intrachain hydrogen bonds between C=O of each peptide bond and the NH of the peptide bond four residues away ...
Document
... There are a large number of disorders, each affecting small numbers of people, where those individuals require much larger amounts of a vitamin or mineral to maintain health, than do people without that metabolic disorder. This would be an interesting topic for class review. ...
... There are a large number of disorders, each affecting small numbers of people, where those individuals require much larger amounts of a vitamin or mineral to maintain health, than do people without that metabolic disorder. This would be an interesting topic for class review. ...
Honors Enzyme reading
... The substrate molecule normally does not fit exactly in the active site. This induces a change in the enzymes conformation (shape) to make a closer fit. In reactions that involve breaking bonds, the inexact fit puts stress on certain bonds of the substrate. This lowers the amount of energy needed to ...
... The substrate molecule normally does not fit exactly in the active site. This induces a change in the enzymes conformation (shape) to make a closer fit. In reactions that involve breaking bonds, the inexact fit puts stress on certain bonds of the substrate. This lowers the amount of energy needed to ...
Click 1
... The aspartic proteases are inhibited by pepstatin. They are also sensitive to diazoketone compounds such as diazoacetyl-D,L-norleucine methyl ester (DAN) and 1,2-epoxy-3-(pnitrophenoxy)propane (EPNP) in the presence of copper ions Cysteine/thiol proteases occur in both prokaryotes and eukaryotes. Ab ...
... The aspartic proteases are inhibited by pepstatin. They are also sensitive to diazoketone compounds such as diazoacetyl-D,L-norleucine methyl ester (DAN) and 1,2-epoxy-3-(pnitrophenoxy)propane (EPNP) in the presence of copper ions Cysteine/thiol proteases occur in both prokaryotes and eukaryotes. Ab ...
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034
... 06. Native gel is used to isolate enzymes. 07. Starch is a homopoloysaccharide. 08. The dipeptide contains one peptide bond. 09. Saturated fatty acids contain double bond. 10. IUB refers to International Union of Biochemistry. III. Complete the following ...
... 06. Native gel is used to isolate enzymes. 07. Starch is a homopoloysaccharide. 08. The dipeptide contains one peptide bond. 09. Saturated fatty acids contain double bond. 10. IUB refers to International Union of Biochemistry. III. Complete the following ...
Chapter 7 (part 2) - University of Nevada, Reno
... groups (fatty acids) are made more water soluble w/CoA attached ...
... groups (fatty acids) are made more water soluble w/CoA attached ...
Amino acids introduction
... Ser, Thr, (Tyr) Met, Cys Phe, Tyr, Trp, (His) Arg, Lys, Asp, Glu, (His) Gly (no R), Pro (cyclic) ...
... Ser, Thr, (Tyr) Met, Cys Phe, Tyr, Trp, (His) Arg, Lys, Asp, Glu, (His) Gly (no R), Pro (cyclic) ...
Week 10 notes
... Levels of Protein Structure • Primary protein structure – linear arrangement of amino acids in the polypeptide (like beads on a string) – exact sequence of amino acids determines overall protein structure (analogy: different arrangements of letters spell out words with different meanings) – all ...
... Levels of Protein Structure • Primary protein structure – linear arrangement of amino acids in the polypeptide (like beads on a string) – exact sequence of amino acids determines overall protein structure (analogy: different arrangements of letters spell out words with different meanings) – all ...
Phenylalanineaminopeptidase of L. pneumophila
... Enzyme assays. Serine endopeptidase assayed at pH 8.0 using L-Pyr-L-Ala-L-Ala-L-Leu-pNA (pNA represents the p-nitroanilide group) as substrate according to the method of Lyublinskaya et a/. (1977). One unit of activity was defined as the amount of enzyme releasing 1 pmol p-nitroalinine min-' at 37 " ...
... Enzyme assays. Serine endopeptidase assayed at pH 8.0 using L-Pyr-L-Ala-L-Ala-L-Leu-pNA (pNA represents the p-nitroanilide group) as substrate according to the method of Lyublinskaya et a/. (1977). One unit of activity was defined as the amount of enzyme releasing 1 pmol p-nitroalinine min-' at 37 " ...
Catalytic triad
A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.