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35 Cards in this Set
- Front
- Back
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__ Bond - Interaction between hydrogen covalently bonded to oxygen, or nitrogen (electronegative element)
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Hydrogen Bonds
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__ Interaction - Electrostatic interactions between two fully charged atoms or groups
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Ionic Interaction
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__ Interactions - associations of nonpolar molecules or groups with each other in aqueous systems
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Hydrophobic
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__ Interactions - transient electrostatic interaction between permanent and/or induced dipoles
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Van der Waals Interactions
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To determine an acids strength, the larger the value of __, the stronger of the acid.
The smaller the __, the stronger the acid. |
Ka
pKa |
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__ is defined as the negative logarithm of the hydrogen ion concentration.
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pH
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__ are solutions that resist changes in pH as an acid or a base is added.
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Buffers
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Most buffers consist of a ___ and its conjugate___.
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Acid
Base |
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__ equation describes hte relationship between the concentration of an acid in solution and the pH of the solution
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Henderson-Hasselbalch
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__ carbons have 4 different groups attached
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Chiral
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__- are compounds that have the same molecular formula but differ in the arrangement of atoms in space
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Stereoisomers
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__ - is an amide bond between 2 amino acids
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Peptide bond
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__ structure - amino acid linear sequence
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Primary Structure
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__ structure - repeating conformations such as alpha-helices and beta-sheets
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Secondary Structure
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__ structure - the shape of the fully folded polypeptide chain
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Tertiary
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__ structure - arrangement of two or more polypeptide chains into multisubnit molecule
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Quaternary
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__ are short amino acid polymers that generally have fewer than 50 amino acid residues
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Peptides
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__ are amio acid polymers with more than 50 amino acid residues
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Polypeptides
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__ is a macromolecule composed of one or more polypeptides
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Protien
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__ bonds help protiens to fold, and are weak in aqueous solutions
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Noncovalent
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Side chains of ___ are nitrogenous bases which are positively charged at nuetral pH, and frequently form ionic interations as well as hydrogen bonds
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Amino Acids
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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.
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Negative
Positive |
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__ enhance reaction rate by lowering the activation energy
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Enzymes
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What are the 4 modes of enzymatic catalysis
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Proximity and Strain Effect
Electrostatic Effects (trasition-state stabilization) Acid-Base Catalysis Covalent Catalysis |
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The binding of the substrate to the enzyme results in formation of the __.
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Enzyme-Substrate Complex
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(Cardinal Number)
duodecim |
Meaning: twelve
Derivative: (none) |
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__ are biological catalysts that are usually protiens, it makes reaching equillibrium faster but the equilibrium constant does not change.
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Enzyme
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Apoenzyme + Cofactor =
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Holoenzyme
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Some enzymes require __ for activity which include: essential ions and coenzymes
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Cofactors
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Enzymes are classified into 6 major groups, name them.
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Oxidoreductases
Transferases Hydrolases Lyases Isomerases Ligases |
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__ the disruption of native conformation of a protien, with loss of biological activity by chemical or physical means.
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Denaturation
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__ Ageants - disrupt noncovalent bonding, resulting in loss of tertiary and quaternary structure (sometimes secondary)
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Deaturing
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__ Protiens - are usually water soluble, and have polypeptide chains that are folding in a spherical shape
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Globular Proteins
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__ Protiens - have polypeptide chains arranged in long strands are are usually insoluable in water.
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Fibrous Proteins
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__ Enzymes have a regulatory site distinct from the active site
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Allosteric
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