structure
the elements that make up protein
Primarily C,H,O, and N, but differs based on R group
What protein generally does inside the cell
Strengthen and protect, send and move messages and cells, catalyze reactions
The amount of types of amino acids
20 different amino acids
The primary structure of a protein shows
tyhe sequence of amino acids
Primary function of enzymes
accelerate chemical reactions (acting as cataclyts but are not consumed in the reaction)
the different polymers
Amino acids chained by peptide bonds (hemoglobin, enzymes, gelatin)
Why protein is needed by other macromolecules
they play crucial roles in their replication, transcription, and translation. Proteins also help maintain the structure and function of other macromolecules by binding to them, transporting them, or catalyzing their reactions.
The n-terminus of an amino acid
the amino end
What links monomers together
peptide bonds through dehydration
Different types of proteins
enzematic, storage, hormonal, contractile, defensive, transport, recepter, and structural
Process that the monomers and polymers are broken and built
Hydrolysis breaks down polymer to monomers and dehydration builds
Engagement with water
Dependent on side chains- some protein parts can mix with water, and other proteins and sides can’t.
The place where essential amino acids are synthesized
outside the body (have to be eaten)
Secondary structure characteristics
Repetitive coil and folds because of hydrogen bonds between repetitive polypeptide backbone
What quaternary structure depicts
two or more polypeptides forming one functional macromolecule (fuller picture)
How different amino acids form different shapes
They are folded into various 3D structures becuase of their R-group. They can bond together or be hydrophobic and therefore form complex structures like an alpha helix or beta plated sheet from h bonds.
How different side chains effect the functions and shape of different proteins
Dictate how they fold and function with the molecules around them- polarity, bonding, changing hydrogen bonding, being hydrophobic
Ionic properties while inside solution
always ionized (at cellular ph)
The amount of polypeptide chains to make one functional macromolecule
one or more
The protein used to fight off disease in the body
defensive
Monomer of protein
Amino acids
What protein does inside the general organism
structural support, catalysis of chemical reactions, transportation of molecules, immune defense, and acting as building blocks for tissues and organs
Most abundant amino acid in human body
Glutamine
the reason for the difference in function of normal vs sickle-cell red blood cells
the proteins aggregate into the fiber, restricting their oxygen holding capacity because of hydrophobic interactions, deforming their shape (Substituting an amino acid for a normal one at the 6th Glucose in primary structure hemoglobin- different chain means different interactions of r chain- different shape = different function)
This protein is responsible for forming the contractile filaments found in muscle cells.
Myosin