Biomolecule Breakdown Crossword Puzzle

QUESTIONS LIST:

• chaperone : a molecular protein, often an hsp, that assists in correct protein folding by binding exposed hydrophobic patches on misfolded intermediates. they utilize atp hydrolysis for energy.
• nterminus : the specific end of a polypeptide chain bearing the free alpha-amino group. it defines the starting direction (n→c) of the protein's linear amino acid sequence.
• pyranose : a six-membered cyclic hemiacetal structure formed when a monosaccharide undergoes an internal reaction. it is derived from the cyclic ether pyran. glucose commonly forms this ring structure.
• ligase : an enzyme class (ec 6) that catalyzes the joining (synthesis) of two molecular substrates into one larger compound. this reaction must be coupled to the cleavage of atp.
• apoenzyme : the inactive protein part of an enzyme complex. it lacks the required non-protein chemical compound (cofactor or coenzyme). when bound, the complex forms the active holoenzyme.
• allostery : the regulation of a multi-subunit protein where ligand binding at one site changes the affinity or activity at distant sites. this often involves a structural shift between tense and relaxed states.
• frameshift : a severe mutation caused by the insertion or deletion of nucleotides where the total number added or removed is not a multiple of three. this alters the subsequent reading frame.
• vitrification : rapid freezing, typically into super-cooled liquid ethane, that creates amorphous, non-crystalline ice. this is essential for preserving the biological structure for cryo-em.
• glycosidic : the specific covalent linkage that joins the anomeric carbon of one monosaccharide to an oxygen atom of another molecule. it links sugar units to form disaccharides or polysaccharides.
• quaternary : the highest order of protein structure, describing the spatial arrangement of multiple polypeptide subunits. it is stabilized mainly by noncovalent forces like hydrophobic effects.