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Exam #1 HBC
| Question | Answer |
|---|---|
| Biochemistry | Chemical composition, metabolism, nutrition, energetic, enzyme function, transfer genetic info, membrane properties, cellular organization and molecular diseases. |
| Vitalism | life and the functions of a living organism depend on a nonmaterial force or principle separate from physical and chemical processes. |
| Who disproved the theory of vitalism? | - Wohler and the urea disproved the theory. From organic to inorganic - Watson and Crick - biological replication in DNA |
| Covalent bond | Strong force, sharing of electron pair by strong adjacent forces. Promotes large molecular diversity. C-C 85 kcal/mol |
| Electrostatic bonding (Salt bridges, salt linkage, ion pair, ionic bond) | attractive and repulsive electrical forces between atoms/ groups of atoms/molecules that are caused both by the presence of ionized species and by the electro(+) and electro(-) properties of the atoms. |
| Hydrogen Bond | weak force, hydrogen atom is covalently linked to an electronegative atom (O or N) in near proximity to another electronegative atom (O or N) |
| Hydrophobic interactions | The attractive force between nonpolar molecules or nonpolar groups which leads to the association of these groups or molecules in an aqueous environment. |
| Van der Waals interactions | 2 uncharged atoms together= electron clouds. Asymmetric/ random variations in the e- positions around one nucleus create transient/opp electric dipole in nearby atom = dipoles weakly attract each other.Closer together, e- clouds repel each other. |
| Weak bonds are? | highly reversible. |
| What is the relationship between ΔG, ΔH, and ΔS. | ΔG = ΔH – TΔS If ΔG = 0, the reaction is at equilibrium If ΔG = +, the reaction is not spontaneous If ΔG = -, the reaction is spontaneous |
| Define and give examples of entropy | Entropy (measure of order) As ΔS increases (ΔS becomes more positive), the products become less ordered (more random). |
| Predict the state of a chemical reaction from the value of ΔG. | If ΔG = 0, the reaction is at equilibrium If ΔG = +, the reaction is not spontaneous If ΔG = -, the reaction is spontaneous |
| Define and discuss potential energy and kinetic energy | Potential energy – The energy stored by matter as a result of its location or spatial arrangement. Kinetic energy – The energy of motion |
| conditions for a spontaneous reaction. | the reactants must have more potential energy than the products and/or be more ordered than the products |
| Gly, Ala, Val, Leu,Ile and Pro are related by? | These aliphatic amino acids are hydrophobic. Notice that proline is the only amino acid whose central carbon atom nitrogen is in a ring. Side chains contain C and/or H |
| Phe, Tyr, Trp are related by? | contain ring structures. Have aromatic R groups and are hydrophobic. OH of tyr can be phosphorylated. |
| Met and Cys are related by? | Contain sulfur. |
| Ser and Thr are related by? | Contain hydroxyl group. The OH can be phosphorylated. Hydrophillic. |
| His, Lis and Arg are related by? | Basic and hydrophillic |
| Asp and Glu are related by? | Acidic and hydrophillic. |
| Asn and Gln are related by? | Contain Amino group and are hydrophillic. |
| Protein | polymer/chain of A.A linked by peptide bond. Protein of 50kD= molec weight 50,000 Daltons. Proteins acan be made up of 20 diff A.A |
| What is the general structure of A.A in non-ionized form? | Amino group, Side chain and carboxyl group. |
| What is the general structure of A.A in ionized form? | Amino group (+), Side chain and carboxyl group(-). |
| Amino Acids | Building block monomers of proteins. Difference in R-groups causes diff phys & chem prop to each A.A. |
| Carboxyl group | Acidic, when it donates a proton it becomes negatively charged. |
| Amino group | Basic, accepts a proton it becomes positively charged. |
| Isoelectric point | pH when molecule has 0 net charge, having a equal number of (+) & (-) charges. Molecule does not move in an electric field. |
| The central carbon in all A.A is asymmetric except for... | Glycine |
| An Amino acid can exist in 2 forms that differ in only the.... | Spatial arrangement of the 4 groups about the central carbon atom. the 2 forms are mirror image of each other and not superimposible. |
| Mirror images that are not super-imposable are | Chiral |
| Enantiomers | 2 molecules are mirror images of each other. |
| Why is Glycine not asymmetrical? | Its R-group is a hydrogen atom. |
| Proteins are made up of only which form? | Left handed form/ L-amino acids. |
| Condensation reaction. | Monomer in, water out. Removal of water. |
| Hydrolysis reation. | Monomer out, water in. Addition of water. |
| Protein macromolecules are formed by ? | Condensation reactions between A.A |
| Although 2 proteins may have the same A.A and are identical in molecular weight, they may be ... | Different molecules. Its in the sequence. Ex: Oxytocin vs. Vasopressin |
| Primary Structure(I) | Described by the type, number and sequence of A.A in the chain. The A.A seq of a protein determines its 3D structure. |
| What is responsible for maintaining the structure of a protein? | Peptide bonds of A.A |
| Secondary Structure (II) | Folding of a polypeptide chain along 1 axis of a molecule into a uniform repeating conformational pattern. |
| What causes the preferential folding of some protein domains into regions with regular, repeating, secondary motifs ? | Combo of intra-molecular H bonds and van der waals forces. |
| What are examples of secondary structural motifs? | Alpha helix and beta sheet. |
| Tertiary Structure (III) | Irregular 3D folding of the polypeptide chain UPON itself. |
| What participates in the stabilizing the tertiary structures of proteins? | Covalent bonding(disulfide bridges), noncovalent interactions( electrostatic/van deer Waals and hydrophobic interactions) |
| Homologs are _____ ? | Descended from a common ancester |
| Two proteins are homologous if they are? | Derived from a common ancestor. |
| Paralogs | Homologs, present within 1 species. DIFFER in detailes biochemical function |
| Orthologs | Homologs, present within DIFFERENT species. Have SIMILAR or IDENTICAL functions. |
| Give examples of orthologs and paralogs. | Orthologs: Bovine ribonuclease (digestive enzyme) and human ribonuclease(digestive enzyme). Paralogs:human ribonuclease(digestive enzyme) and Angiogenin(stimulates blood vessal growth) |
| Quaternary Structure (IV) | Results from the interaction between individual polypeptide chainds to yeiled larder aggregates (multimers) |
| What can stabilize the subunit structure of the quaternary structure? | Covalent bridges and especially non-covalent interactions (electrostatic/van deer Waals and hydrophobic interactions) |
| 3D structure determines a proteins? | FUNCTION |
| Denaturation | Loss of 3D structure to cause a loss of function. The process is considered as an unfolding og the protein molecule. The can be denatured by heat, extreme pH change or chemicals. |
| Renaturation | Process by which a protein can regain its native structure and its bio activity/ function. |
Created by:
jstanczak
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