Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
36 Cards in this Set
- Front
- Back
2, 3-bisphosphoglycerate (2,3-BPG)
|
Enhance delivery of oxygen by hemoglobin
|
|
Allosteric Effector or Modulator
|
A biomolecule that binds to the regulatory site of an allosteric protein and thereby modulates its activity
|
|
Allosteric Interaction
|
The modulation of activity of a protein that occurs when a molecule binds to the regulatory site of the protein
|
|
Allosteric Protein
|
A protein whose activity is modulated by the binding of another molecule
|
|
Bohr Effect
|
The phenomenon observed when exposure to carbon dioxide, which lowers the pH inside the cells, causes the oxygen affinity of hemoglobin in red blood cells to decrease
|
|
Carbamate Adduct
|
Carbon dioxide is carried in the hemoglobin in this form
|
|
Conformation
|
any three-dimensional structure, or spatial arrangement, of a molecule that results from rotation of functional groups around single bonds. Can assume many of these
|
|
Cooperativity of Folding
|
The phenomenon whereby formation of structure in one part of a macromolecule promotes the formation of structure in the rest of the molecule
|
|
Denaturation
|
A disruption in the native conformation of a biological macromolecule that results in loss of the biological activity of the macromolecule
|
|
Domain
|
A discrete, independent folding unit within the tertiary structure of a protein. Combinations of several motifs
|
|
Fibrous Protein
|
A major class of water-insoluble proteins that associate to form long fibers. Physically tough and provide mechanical support
|
|
Fold
|
A combination of secondary structures that form the core of a protein domain
|
|
Globular Protein
|
A major class of proteins, many of which are water soluble. Compact and roughly spherical, containing tightly folded polypeptide chains
|
|
Hairpin Loop
|
A secondary structure adopted by single-stranded polynucleotides that arises when short regions fold back on themselves and hydrogen bonds form between complementary bases
|
|
Heat Shock Proteins
|
A protein whose synthesis is increased in response to stresses such as high temperature. many are chaperones
|
|
Loop
|
A non-repetitive polypeptide region that connects secondary structures within a protein molecule and provides directional changes necessary for a globular protein to attain its compact shape
|
|
Molecular Chaperone
|
A protein that forms complexes with newly synthesized polypeptide chains and assists in their correct folding into biologically functional conformations
|
|
Monomer
|
A small compound that becomes a residue when polymerized with other monomers
|
|
Motif
|
A combination of secondary structure that appears in a number of different proteins
|
|
Oligomers
|
A multi subunit molecule whose arrangement of subunits always has a defined stoichiometry and almost always displays symmetry
|
|
Oxygenation
|
The reversible binding of Oxygen to a macromolecule
|
|
Peptide Group
|
The nitrogen and carbon atoms involved in a peptide bond and their four substituents; the carbonyl oxygen atom, the amide hydrogen atom, and the two adjacent a-carbon atoms
|
|
Pitch
|
The axial distance for one complete turn of a helical structure
|
|
Positive cooperativity of binding
|
There is one binding site per subunit for each ligand, that the conformation of each subunit is constrained by its association with other subunits
|
|
Primary Structure
|
The sequence in which residues are covalently linked to form a polymeric chain
|
|
Proteomics
|
the entire complement of proteins that is or can be expressed by a cell, tissue or organism
|
|
Quaternary Structure
|
The organization of two or more polypeptide chains within a multisubunit protein
|
|
R State
|
One conformation of Hemoglobin, facilitates oxygen binding oxy conformation
|
|
T State
|
One Conformation of Hemoglobin which resists oxygen binding deoxy conformation
|
|
Secondary Structure
|
is maintained by hydrogen bonds between carbonyl carbons and amide groups of the backbone.
|
|
Tertiary Structure
|
The compacting of polymeric chains into one or more domains within a macromolecule. Stabilized by hydrophobic interactions between side chains
|
|
Turns
|
Short loops of up to 5 residues
|
|
Alpha helix
|
A common secondary structure of proteins, in which the carbonyl oxygen of each amino acid residue forms a hydrogen bond with the amide hydrogen of the fourth residue further toward the C-terminus of the polypeptide chain
|
|
B-pleated Sheet
|
Planar peptide group meet each other at angles like the folds in an accordion
|
|
B sheet
|
A common secondary structure of proteins that consists of extended polypeptide chains stabilized by hydrogen bonds between the carbonyl oxygen of one peptide bond and the amide hydrogen of another on the same or an adjacent polypeptide chain. Nearly perpendicular which may be parallel or antiparallel
|
|
B strand
|
An extended polypeptide chain within a B sheet secondary structure or having the same conformation as a strand within a B sheet
|