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35 Cards in this Set

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__ Bond - Interaction between hydrogen covalently bonded to oxygen, or nitrogen (electronegative element)
Hydrogen Bonds
__ Interaction - Electrostatic interactions between two fully charged atoms or groups
Ionic Interaction
__ Interactions - associations of nonpolar molecules or groups with each other in aqueous systems
Hydrophobic
__ Interactions - transient electrostatic interaction between permanent and/or induced dipoles
Van der Waals Interactions
To determine an acids strength, the larger the value of __, the stronger of the acid.
The smaller the __, the stronger the acid.
Ka

pKa
__ is defined as the negative logarithm of the hydrogen ion concentration.
pH
__ are solutions that resist changes in pH as an acid or a base is added.
Buffers
Most buffers consist of a ___ and its conjugate___.
Acid

Base
__ equation describes hte relationship between the concentration of an acid in solution and the pH of the solution
Henderson-Hasselbalch
__ carbons have 4 different groups attached
Chiral
__- are compounds that have the same molecular formula but differ in the arrangement of atoms in space
Stereoisomers
__ - is an amide bond between 2 amino acids
Peptide bond
__ structure - amino acid linear sequence
Primary Structure
__ structure - repeating conformations such as alpha-helices and beta-sheets
Secondary Structure
__ structure - the shape of the fully folded polypeptide chain
Tertiary
__ structure - arrangement of two or more polypeptide chains into multisubnit molecule
Quaternary
__ are short amino acid polymers that generally have fewer than 50 amino acid residues
Peptides
__ are amio acid polymers with more than 50 amino acid residues
Polypeptides
__ is a macromolecule composed of one or more polypeptides
Protien
__ bonds help protiens to fold, and are weak in aqueous solutions
Noncovalent
Side chains of ___ are nitrogenous bases which are positively charged at nuetral pH, and frequently form ionic interations as well as hydrogen bonds
Amino Acids
An amino acid will have a __ charge is the pH of the solution is above its pI; it will have __ charge is the pH of the solution is below its pI.
Negative

Positive
__ enhance reaction rate by lowering the activation energy
Enzymes
What are the 4 modes of enzymatic catalysis
Proximity and Strain Effect
Electrostatic Effects (trasition-state stabilization)
Acid-Base Catalysis
Covalent Catalysis
The binding of the substrate to the enzyme results in formation of the __.
Enzyme-Substrate Complex
(Cardinal Number)

duodecim
Meaning: twelve

Derivative: (none)
__ are biological catalysts that are usually protiens, it makes reaching equillibrium faster but the equilibrium constant does not change.
Enzyme
Apoenzyme + Cofactor =
Holoenzyme
Some enzymes require __ for activity which include: essential ions and coenzymes
Cofactors
Enzymes are classified into 6 major groups, name them.
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
__ the disruption of native conformation of a protien, with loss of biological activity by chemical or physical means.
Denaturation
__ Ageants - disrupt noncovalent bonding, resulting in loss of tertiary and quaternary structure (sometimes secondary)
Deaturing
__ Protiens - are usually water soluble, and have polypeptide chains that are folding in a spherical shape
Globular Proteins
__ Protiens - have polypeptide chains arranged in long strands are are usually insoluable in water.
Fibrous Proteins
__ Enzymes have a regulatory site distinct from the active site
Allosteric