Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Biochemistry
Exam 1
| Term | Definition |
|---|---|
| (α) Alpha-carbon | Carbon next to the carboxyl group. Connected to the amine and the R-group |
| Resonance Structures | Multiple arrangements of single and double bonds |
| Disulfide Bonds | Polypeptide chains can be cross-linked by? |
| Three fields of biochemistry | 1.) Structural Biology 2.) Enzymology 3.) Metabolism |
| ΔG°′ | The standard free energy change at pH 7. |
| ΔG° | The standard free energy change under standard conditions, i.e. 1 atm pressure, 298 K, in a concentration of 1.0M |
| Spontaneous | If ΔG is negative, then the reaction is? |
| All amino acids contain: | 1.) Carboxylic acid group 2.) alpha amino group 3.) R=side chain |
| Dipole | A molecule or bond with opposite charges at either end |
| Codons | Each amino acid is encoded by one or more specific sequences of three nucleotides |
| pH | The concentration of hydrogen ions in a solution |
| Enzymes | Act as catalysts for chemical transformation. Convert energy from one form to another. |
| V(o) | Initial velocity of rate of catalysis when the reaction is just beginning. t~0 |
| Allosteric Enzymes | The binding of substrate to one active site can alter the properties of other active sites in the same enzyme molecule. |
| Nonspontaneous | If ΔG is positive, then the reaction is? |
| Holoenzyme | An enzyme/apoenzyme with its cofactor |
| Proteins | Cellular machines performing mechanical work that drives cellular processes |
| Transition State | A molecular form that is no longer substrate but not yet product. |
| Classes of amino acids | 1.) Hydrophobic (non-polar) 2.) Polar neutral 3.) Positively charged (basic) 4.) Negatively charged (acidic) |
| Intermolecular | Forces that exist between molecules |
| Primary Structure of Proteins | Amino acids bind to each other to form chains. Chains are linked peptide bonds to form polypeptide chains. |
| Zwitterions | Free amino acids in a solution at neutral pH |
| Michaelis- Menten Kinetics | Rate of an enzyme-catalyzed reaction is proportional to the amount of the enzyme-substrate complex |
| Larger | The more exergonic (releases energy) a reaction is, the _________ the equilibrium constant k'(eq) will be |
| Apoenzyme | An enzyme without its cofactor |
| Covalent Bond | Two elements share an electrons. Strongest type of bond. |
| Activation Energy | Difference in free energy between the transition state and the substrate |
| Proteolytic Enzymes | Catalyze the hydrolysis of peptide bonds |
| k(m) "The Michaelis Constant" | The concentration of substrate at which half the active sites of the enzyme are filled |
| V(max) | Maximal rate of enzymatic reaction. Attained when the catalytic sites on the enzyme are saturated with substrate. |
| Key Properties of Proteins | 1.) Linear polymers composed of amino acids 2.) Wide variety of functional groups 3.) Can interact with one another to form complexes 4.) Rigid or flexible |
| pH>pKa | Compound/functional group will exist in more deprotonated form (conjugate base). High pH= more H+ acceptor |
| Basic | When the pH of the environment is greater than the pKa of the compound, the environment is considered? |
| Ionic Bonds | Transfer of electrons from one element to another |
| Peptide Bond Qualities | 1.) Partial double bond due to resonance 2.) Flexible yet conformationally restricted 3.) Almost all have trans configuation |
| Intrinsically Unstructured Proteins | Do not have a defined structure under physiological conditions until they interact with other molecules |
| Metamorphic Proteins | Exist in an ensemble of structures of approximately equal energies that are in equilibrium |
| Cofactors | Small molecules some enzymes need for activity. Two types: Coenzymes and metals |
| -1/k(m) | Lineweaver-Burk Plot: X-intercept i= |
| Amphipathic |
Created by:
krv.cell
Popular Biochemistry sets