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There are multiple places for __________ bonds to form in a protein.
non covalent
primary structure is ______ bond and ___ bond
peptide and covalent
proline can’t form _____
alpha helix
bulky or too cracked side chain can’t form
alpha helix
Side chain interactions are important in the __________ and __________ structure of proteins.
tertiary, quaternary
Electrostatic interactions can occur between side chains, such as __________ bonds and __________ bonds.
ionic, hydrogen
Hydrophobic amino acids can interact to form a __________ core inside of a protein.
hydrophobic
The carbonyl oxygen from a polypeptide bond can form __________ bonds with the hydrogen from the amide group.
hydrogen
Proteins in the cytosol are characterized by a predominance of __________ amino acids on their exterior.
hydrophilic
In a protein membrane, __________ amino acids will interact with lipids.
hydrophobic
A protein with two or more subunits has __________ structure.
quaternary
The primary structure of a protein is formed by __________ bonds.
peptide
Alpha helices and beta sheets are examples of __________ structures in proteins.
secondary
Hydrogen bonds in a helix form between the carbonyl oxygen and the nitrogen of the __________ group.
amide
In a parallel beta sheet, all peptide strands run in the __________ direction.
same
An example of a protein needing proteolytic cleavage to be functional is __________.
proinsulin(pro-protein)
The tertiary structure of a protein is dominated by __________ interactions among side chains.
non covalent
The covalent bond formed between two cysteine residues is called a __________ bond.
disulfide
Quantinary structure is characterized by the presence of more than __________ subunit(s).
one
The functional group crucial for oxygen transport in hemoglobin is called a __________ group.
prosthetic
Proteins are formed from chains of __________ linked by peptide bonds.
amino acids
During protein synthesis, the amino terminus of polypeptides emerges first from the __________.
ribosome
The process by which proteins fold into their functional shape is influenced by chaperone proteins, which help mask certain __________.
amino acids
Non-covalent interactions contribute to the stability of protein structures, analogous to __________.
molecular Velcro
In aqueous environments, soluble proteins exhibit __________ amino acids on their outer surfaces.
polar or charged
beta sheets are formed by ______ betweeen peptide backbones
hydrogen bond
parallel beta sheets
N-C all in same direction
anti-parallel
N-C in opposite directions