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Exam #1 HBC

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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