Amino Acid Structure Overview

What is the basic structure of an amino acid?

What is the function of amino acids in the body?

What are proteins primarily responsible for in the cell?

What is unique to each amino acid?

Which functional groups are present in every amino acid molecule?

What type of bond does the α-carbon atom of an amino acid typically form with the R group?

What is the primary function of proteins in the cell?

What is the significance of the α-carbon atom in an amino acid?

Which of the following is a function of proteins in the cell?

What is the role of antibodies in the form of proteins?

Which statement about proteins is accurate?

What is the function of interferon, a form of protein?

What is a key role of proteins in gene expression?

What is the primary function of interferon, a form of protein?

Which statement about the role of proteins in gene expression is accurate?

What is a key role of proteins in binding cells together into tissues?

What do proteins primarily protect animals from, when in the form of antibodies?

What is the main function of proteins in enabling movement?

How many different combinations of proteins are possible with 20 amino acids when considering a dipeptide made of just two amino acids joined together?

What is the formula to calculate the number of different combinations possible with 20 amino acids for a protein with n amino acids in the chain?

What type of reaction links together amino acids to form proteins?

What gives each protein a characteristic and unique sequence of amino acids?

What is the formula to calculate the number of different combinations possible with 20 amino acids for a protein with $n$ amino acids in the chain?

If a protein has a chain of 4 amino acids, how many different combinations are possible with 20 amino acids?

What does a dipeptide made of just two amino acids joined together yield in terms of different combinations?

If a protein has a chain of 6 amino acids, how many different combinations are possible with 20 amino acids?

What is the significance of the unique sequence of amino acids in a protein?

Which level of protein structure is primarily responsible for giving identity and characteristics to a protein?

What determines the shape of a protein?

What allows amino acids to interact with each other that are not close in primary structure?

What is the primary distinction between the terms 'polypeptide' and 'protein'?

When is the term 'protein' generally used?

What does the term 'polypeptide' specifically refer to?

What is the primary distinction between the terms 'polypeptide' and 'protein'?

What allows amino acids to interact with each other that are not close in primary structure?

What determines the shape of a protein?

What allows proteins to be amazing catalysts and adapt to, respond to, and pass on signals upon binding of other molecules or proteins?

What happens if the structure of a protein is altered?

What characteristic defines proteins in terms of structure?

What allows proteins to be amazing catalysts and adapt to, respond to, and pass on signals upon binding of other molecules or proteins?

What happens if the structure of a protein is altered?

What is the primary distinction between the terms 'polypeptide' and 'protein'?

What is the end of the protein that contains the only free α-carboxyl group called?

Where does the synthesis of proteins occur?

How does the synthesis of proteins proceed?

What is the end of the protein that has the free α-amino group referred to as?

Where does the synthesis of proteins occur?

What is the primary function of the carboxyl terminus in a protein?

What is the primary reason for arranging R-groups in an alternating orientation on either side of the polypeptide chain?

What can occur when consecutive R-groups are oriented on the same side of a peptide backbone?

What is the significance of organizing R-groups in an alternating orientation on either side of the polypeptide chain?

Why is the organization of R-groups in a protein not random?

What is the primary consequence of consecutive R-groups being oriented on the same side of a peptide backbone?

In what manner are sequential R-groups arranged around a peptide bond?

What is the primary determinant of the overall conformation of a protein?

What directly specifies the sequence of amino acids in proteins?

What is the result of mutation and selection over evolutionary time?

What are regions of DNA specifying proteins known as?

What is the ultimate determinant of the overall conformation of a protein?

What directly specifies the sequence of amino acids in proteins?

What are regions of DNA specifying proteins known as?

What arrived at the current state of the primary structure of any protein?

What is the primary determinant of the overall conformation of a protein?

What directly specifies the sequence of amino acids in proteins?

What are regions of DNA specifying proteins known as?

What is the result of mutation and selection over evolutionary time?

What gives rise to the properties a protein has?

At the tertiary level of protein structure, what plays a role in folding?

What brings amino acids close together that are not near each other in primary structure?

What gives rise to folds that bring amino acids close together that are not near each other in primary structure?

What is the primary role of the sequence of amino acids in determining a protein's properties?

Which level of protein structure involves individual components of secondary structure interacting with each other?

What stabilizes a globular protein?

What treatments can cause a protein to unfold and lose its structure and function?

What gives rise to distinct 3-D shapes in non-fibrous proteins?

Which of the following is a force that stabilizes a globular protein?

What effect do treatments like heat, pH changes, detergents, and urea have on a globular protein?

What gives rise to distinct 3-D shapes in non-fibrous proteins?

Which force stabilizes protein structure as a result of interactions that favour the exclusion of water?

What type of bonds are made when two sulfhydryl side-chains of cysteine are brought into close proximity?

Which force arises as a result of ionization of R-groups in the amino acids comprising a protein?

What kind of forces can give rise to regular repeating structures, such as helices or pleats, in proteins?

What type of bond is made when two sulfhydryl side-chains of cysteine are brought into close proximity?

What type of interactions stabilize protein structure as a result of interactions that favor the exclusion of water?

What type of forces are generally weak in comparison to covalent bonds and are dynamic due to the fluctuating nature of the attraction?

Which force between amino acids that are close to each other in primary structure can give rise to regular repeating structures, such as helices or pleats, in proteins?

Which force arises as a result of ionization of R-groups in the amino acids comprising a protein?

What is the term used to describe various weak interactions that are generally weak in comparison to covalent bonds?

What type of bond can give great strength to the overall protein structure when two sulfhydryl side-chains of cysteine are brought into close proximity?

Which force stabilizes protein structure as a result of interactions favoring the exclusion of water?

What type of forces stabilize protein structure as a result of interactions that favor the exclusion of water?

Which type of bond is made when two sulfhydryl side-chains of cysteine are brought into close proximity, covalently joining different protein regions and giving great strength to the overall structure?

Which force arises as a result of ionization of R-groups in the amino acids comprising a protein?

What kind of forces can give rise to regular repeating structures, such as helices or pleats, in proteins?

Which type of interaction favors the exclusion of water and stabilizes protein structure?

What term is used to describe various weak interactions that are generally weak in comparison to covalent bonds?

What gives great strength to the overall protein structure when two sulfhydryl side-chains of cysteine are brought into close proximity?

Which force is dynamic due to the fluctuating nature of the attraction and is generally weak in comparison to covalent bonds?

What might be a consequence of protein misfolding?

Which diseases are associated with protein misfolding?

Which tissue is often affected by misfolding diseases?

What might be a consequence of protein misfolding?

Which diseases are associated with protein misfolding?

Which tissue is often affected by misfolding diseases?

What are the two classes of proteins used by cells to facilitate proper folding of proteins?

Why do cells expend energy to facilitate the proper folding of proteins?

What is the primary role of molecular chaperones in cells?

What is a key characteristic of proteins with quaternary structure?

Which protein demonstrates quaternary structure?

How do myoglobin and hemoglobin differ in terms of subunit structure?

What gives rise to differences in the behavior towards oxygen between myoglobin and hemoglobin?

What is the primary difference between myoglobin and hemoglobin in terms of structure?

What is a key characteristic of proteins with quaternary structure?

What gives rise to differences in the behavior towards oxygen between myoglobin and hemoglobin?

Which protein demonstrates quaternary structure?

What is the primary distinction between myoglobin and hemoglobin?

What allows proteins to be amazing catalysts and adapt to, respond to, and pass on signals upon binding of other molecules or proteins?

Which amino acid is known for its unique ability to function in both acid and base catalysis near physiological pH values?

Which group of amino acids are often found clustered on the surface of globular proteins in aqueous solutions due to their hydrophilic nature?

Which amino acid is most often found in the active sites of protein enzymes?

Which chemical property sets histidine apart from the other standard amino acids?

Which type of amino acids are precursors of nitrogenous base components of nucleotides and nucleic acids?

Which amino acid derivative acts as a neurotransmitter?

Which type of amino acids are often found clustered on the surface of globular proteins in aqueous solutions?

Which chemical reaction is particularly important due to its effect on protein structure?

What is the primary role of heme, a complex amino-acid derived cofactor?

What distinguishes nonstandard amino acids from standard amino acids?

Which group of amino acids is characterized as hydrophobic?

Which amino acids possess functional groups with electron pairs available for hydrogen bonding to water and other molecules?

Which amino acids have a carboxylic acid on their side chains that gives them acidic properties?

Which group of amino acids plays a central role in amino acid metabolism?

Which type of amino acids will ionize in an aqueous solution at physiological pH?

Which group of amino acids has R groups possessing a spectrum of functional groups?

Which group of amino acids has either aliphatic or aromatic R groups?

Which group of amino acids is characterized by being hydrophobic ('water fearing')?

Which group of amino acids has side chains that will fold into a three-dimensional shape to bury hydrophobic side chains in the protein interior in aqueous solutions?

Which group of amino acids possess at least one atom (nitrogen,oxygen,sulfur) with electron pairs available for hydrogen bonding to water and other molecules?

Which amino acid is known for its ability to function in both acid and base catalysis near physiological pH values?

What is the most abundant excitatory neurotransmitter in the central nervous system?

Which group of amino acids are often found clustered on the surface of globular proteins in aqueous solutions?

Which amino acid is most often found in the active sites of protein enzymes?

Which amino acid is a precursor of serotonin and melatonin, and synthesized from histidine?

Which type of amino acids refers to those that have been chemically modified after incorporation into a protein?

Which group of amino acids possess at least one atom with electron pairs available for hydrogen bonding to water and other molecules?

What is the primary role of the sequence of amino acids in determining a protein's properties?

What are some precursors of a variety of complex nitrogen-containing molecules?

What type of forces can give rise to regular repeating structures, such as helices or pleats, in proteins?

Which group of amino acids has side chains that are hydrophobic ('water fearing')?

Which group of amino acids possess at least one atom (nitrogen, oxygen, sulfur) with electron pairs available for hydrogen bonding to water and other molecules?

Which two amino acids have carboxylic acid on their side chains, giving them acidic (proton-donating) properties?

Which group of amino acids will ionize in an aqueous solution at physiological pH, giving an overall charge of −1?

What type of functional groups do most amino acids in Group II possess?

What is the primary characteristic of Group I amino acids?

What is the distinguishing feature of Group III acidic amino acids?

What is the primary property of Group II polar, uncharged amino acids in aqueous solutions?

Which amino acid is known for its unique ability to function in both acid and base catalysis near physiological pH values?

Which group of amino acids possess at least one atom with electron pairs available for hydrogen bonding to water and other molecules?

Which amino acid is most often found in the active sites of protein enzymes?

What type of amino acids are often found clustered on the surface of globular proteins in aqueous solutions?

What are nonstandard amino acids known for?

What is the primary role of Group II amino acids in proteins?

What is the significance of histidine's imidazole side chain?

What is the primary function of arginine, histidine, and lysine?

What are some prominent nitrogen-containing molecules that amino acids are precursors of?

What kind of reactions can amino acids undergo via their various chemical functionalities?

Which group of amino acids is characterized by having side chains with electron pairs available for hydrogen bonding to water and other molecules?

Which amino acid group has R groups that are hydrophobic ('water fearing') due to their aliphatic or aromatic nature?

Which two amino acids have carboxylic acid on their side chains that give them acidic (proton-donating) properties?

Which group of amino acids possess at least one atom (nitrogen, oxygen, or sulfur) with electron pairs available for hydrogen bonding to water and other molecules?

What is the charge of the acidic amino acids aspartate and glutamate in an aqueous solution at physiological pH?

What type of R groups do nonpolar amino acids in Group I have that makes them hydrophobic?

What is the primary distinguishing characteristic of polar, uncharged amino acids in Group II?

What property of the side chains of nonpolar amino acids in Group I leads to their burial in the protein interior in aqueous solutions?

What role do polar, uncharged amino acids play in the folding of globular proteins in aqueous solutions?

Which amino acid is capable of functioning in both acid and base catalysis near physiological pH values?

Which group of amino acids is often found clustered on the surface of globular proteins in aqueous solutions?

Which amino acid group is characterized by having side chains with electron pairs available for hydrogen bonding to water and other molecules?

Which reaction is particularly important due to its effect on protein structure?

Which complex nitrogen-containing molecule are amino acids precursors of?

Which amino acid is a precursor of serotonin and melatonin, and synthesized from histidine?

What is the primary reason for arranging R-groups in an alternating orientation on either side of the polypeptide chain?

What are nonstandard amino acids primarily referred to as?

What is the primary role of heme, a complex amino-acid derived cofactor?

What gives rise to folds that bring amino acids close together that are not near each other in primary structure?

Which group of amino acids has R groups that are hydrophobic ('water fearing') due to their aliphatic or aromatic nature?

Which type of amino acids will ionize in an aqueous solution at physiological pH?

What is the distinguishing feature of Group III acidic amino acids?

Which group of amino acids possess at least one atom with electron pairs available for hydrogen bonding to water and other molecules?

What directly specifies the sequence of amino acids in proteins?

Which force stabilizes protein structure as a result of interactions favoring the exclusion of water?