At the _______ level of protein structure, a linear sequence of amino acids is joined by peptide bonds to form a polypeptide.
Back
Dehydration synthesis
Front
Reaction in which two molecules are covalently bonded, with the loss of a water molecule
Back
Tertiary
Front
At the ________ level of protein structure, various chemical associations in precise regions of a polypeptide cause it to fold into a 3D shape that will determine its function.
Back
Glycosidic linkage
Front
In carbohydrates, monosaccharides are joined together in a covalent bond called __________ _______.
Back
Chaperonins
Front
Assist in the proper folding of the protein by keeping the polypeptide segregated from disruptive chemical conditions in the cytoplasmic and create a hydrophilic environment for folding polypeptides
Back
20
Front
# different amino acids which can assemble according to genetic code to make different proteins.
Back
Unsaturated fats
Front
Fats with one or more double covalent bonds, which is less likely to solidify and more flexible.
Back
Monosaccharide
Front
EX: monomer Glucose
Back
3D structure
Front
The amino acid sequence ultimately determine the __ _________ of proteins.
Back
Secondary
Front
At the _________ level of protein structure, hydrogen bonds form between the partial positive hydrogen atom of amine groups and the partial negative oxygen atom of carboxyl groups.
Back
Polypeptide
Front
The polymer in a protein is a(n) ___________.
Back
Quaternary
Front
At the __________ level of protein structure, 2 to 4 completely formed polypeptides combine.
Back
Macromolecules
Front
Carbohydrates, proteins, lipids, and nucleic acids
Back
Steroid
Front
Lipid characterized by a carbon skeleton consisting of hydrogen-fused rings.
Back
Phospholipid
Front
Basic structural component of cell membranes, with a polar/hydrophilic head region and a nonpolar/hydrophobic tail region, giving membranes their selective permeability.
Back
Denaturation
Front
Excessive heat can cause ____________, in which a protein unravels and loses its native shape.
Back
Sickle cell anemia
Front
In this disease, one amino acid at the primary level (valine) replaces glutamic acid and the result is a distorted shape at the subsequent levels.
Back
HDL
Front
Good cholesterol is called ___ ____________.
HINT: Keep your ____ HIGH :-)
Back
Structure
Front
A protein's _________ determines its function.
Back
Amino acid
Front
The monomer in a protein is a(n) _____ ____.
Back
Polysaccharide
Front
Three or more monosaccharides linked together form a ______________.
Back
LDL
Front
The bad cholesterol, which can harden in arteries.
HINT: Keep your ____ LOW :-)
Back
Lipids
Front
Cushioning of organs, insulation, and energy storage are three functions of ___________.
Back
α Helix
Front
___ ___________ are a secondary structure found in proteins.
Back
Hydrolysis
Front
Pocess that is the reverse of dehydration synthesis. In __________, or water breakage, the bond between monomers is broken by the addition of a water molecule.
Back
β Pleated Sheet
Front
__ ___________ ______________ are a secondary structure found in proteins.
Back
Polymers
Front
Long molecules consisting of many similar or identical building blocks linked by covalent bonds.
Back
Monosaccharides
Front
Carbohydrates polysaccharides are made up of _______________.
Back
Disaccharide
Front
Two monosaccharides covalently bonded form a ____________.
EX: Sucrose
Back
Cellulose
Front
example of a structural carbohydrates
Back
Nucleotides
Front
Nucleic acids are composed of ___________.
Back
starch
Front
stored carbohydrate/polysaccharide in plants
Back
Receptor
Front
________ proteins are embedded in all membranes and allow cells to interact with molecules and other cells.
Back
Glycogen
Front
Stored carbohydrate/polysaccharide in animals
Back
Polynucleotide
Front
The polymer in a nucleic acid is a(n) ______________.
Back
Amino; carboxyl; R
Front
Amino acids are formed of a(n) _____ group with a(n) ________ group and a(n) _ group side chain.
