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If a protein contains three polypeptide chains that are held together by bonding forces what kind of structure does the protein have?
The protein has a quaternary structure.
In addition, each polypeptide chain has a primary, secondary, and tertiary structure.
The primary structure is the sequence of amino acids in a chain.
The secondary structure is the next higher level of arrangement of a chain in space, for example coiling into a alpha-helix, shaping into a beta-pleated sheet, or forming into a turn or loop.
Tertiary structure is a yet higher-level folding of the chain into its final three-dimensional shape.
Some proteins have only one chain, but if there are two or more, the combination of these chains to form the functional protein is the quaternary structure.
What else can I help you with?
What are the forces which create the tertiary structure of a polypeptide?
The tertiary structure of a polypeptide is primarily determined by interactions between the R-groups of amino acids in the protein. These interactions include hydrogen bonding, disulfide bonds, hydrophobic interactions, and electrostatic interactions. The overall folding of the polypeptide chain into its tertiary structure is crucial for the protein's function.
What is the level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide?
The level of protein structure that describes the three-dimensional folding of a polypeptide is the tertiary structure. It includes interactions between secondary structural elements (like alpha helices and beta sheets) to give the protein its unique three-dimensional shape.
Where does tRNA move after this bonding of lysine to the polypeptide?
After bonding lysine to the polypeptide chain, the tRNA moves away from the ribosome as it is no longer needed for the process of translation. The ribosome then moves along the mRNA to the next codon, where another tRNA molecule carrying the next amino acid will come in to continue building the polypeptide chain.
The sequence of amino acids joined together refers to the?
Peptide sequence or amino acid sequence is the order in which amino acid residues, connected by peptide bonds, lie in the chain in peptides and proteins. The sequence is generally reported from the N-terminal end containing free amino group to the C-terminal end containing free carboxyl group. Peptide sequence is often called protein sequence if it represents the primary structure of a protein.
How does the shape of a protein change as it goes from primary to quaternary?
Quaternary structure of a protein means that the protein contains more than one polypeptide chains. Those chains interact with each other to maintain the protein's shape, providing stability to the protein. The interactions are covalent, (disulfide bonds) and non-covalent, like Hydrogen bonds, electrostatic forces, hydrophobic forces. Because of these interactions, all protein with quaternary structure, has three- dimensional shape, (either globular or fibrous).
Which primarily responsible for the helical structure of a polypeptide chain?
The primary structure of a polypeptide chain, consisting of a sequence of amino acids, is primarily responsible for the helical structure of a polypeptide chain. In particular, the recurring hydrogen bonding between the carbonyl oxygen of one residue and the amide hydrogen of another residue stabilizes the helical conformation, leading to the formation of an alpha helix.
A pleated sheet organization in a polypeptide chain is an example of which structure?
A pleated sheet organization in a polypeptide chain is an example of secondary protein structure, specifically beta sheet secondary structure. It involves hydrogen bonding between neighboring polypeptide strands running in opposite directions.
What are the forces which create the tertiary structure of a polypeptide?
The tertiary structure of a polypeptide is primarily determined by interactions between the R-groups of amino acids in the protein. These interactions include hydrogen bonding, disulfide bonds, hydrophobic interactions, and electrostatic interactions. The overall folding of the polypeptide chain into its tertiary structure is crucial for the protein's function.
What structure describes the alpha-helices and beta-sheets that are formed by hydrogen bonding vetween backbone atoms located near each other in the polypeptide chain?
This bonding is done in the secondary structure of the protein.
What is the level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide?
The level of protein structure that describes the three-dimensional folding of a polypeptide is the tertiary structure. It includes interactions between secondary structural elements (like alpha helices and beta sheets) to give the protein its unique three-dimensional shape.
Differentiate between secondary and tertiary structure by describing the parts of the polypeptide chain that participates in the bonds that hold together each level of structure?
Secondary structure refers to local folding patterns involving hydrogen bonding between the peptide backbone, forming alpha helices or beta sheets. Tertiary structure involves the overall 3D folding of the entire polypeptide chain, with interactions between side chains such as hydrophobic interactions, hydrogen bonding, disulfide bridges, and electrostatic interactions playing a major role in maintaining the structure.
What is a difference in the structure of proteins and polysaccharides?
Polysaccharides are essentially many carbon sugar "rings" linked together. They are carbohydrates, and our bodies break them down into monosaccharides (single "rings") to gain energy. To provide energy is their main function. In contrast, a peptide bond is formed between two amino acids via dehydration synthesis. Amino acids are the monomers for proteins within the body, who function in part to catalyze reactions and carry out other directions of DNA. Many peptide bonded amino acids = a polypeptide. The most basic difference would be that polypeptides are proteins, where as polysaccharides are carbohydrates.
What is the difference between the structure of a protein and an amino acid?
think of it like legos. single Lego pieces are like amino acids and they get bonded together to form a longer chain called a polypeptide. polypeptides bind to other polypeptides by hydrogen bonding to each other and form a protein with structure.
The characteristic globular shape of a polypeptide is?
determined by its amino acid sequence and interactions between amino acid side chains. The folding of the polypeptide into a specific shape is influenced by factors such as hydrogen bonding, disulfide bridges, and hydrophobic interactions. This globular shape is essential for the proper functioning of proteins in cells.
The backbone of a polypeptide could be represented by?
The backbone of a polypeptide could be represented by a chain of nitrogen and hydrogen atoms. The polypeptide backbone is the key contributor to protein secondary structure, which involves backbone-to-backbone hydrogen bonding.
Some regions of a polypeptide may coil or fold back on themselves?
Yes, certain regions of a polypeptide chain can coil or fold back on themselves due to interactions between amino acids within the chain. These interactions, such as hydrogen bonding and hydrophobic interactions, help stabilize the folded structure of the protein, ultimately determining its function.
What characteristic of amino acids determine the primary structure of proteins - Acid-base properties - Side chain composition - Hydrogen bonding properties - Sequence in polypeptide chains?
If you are asking which of the four following answers determines the primary structure of proteins, the answer would be d) sequence of polypeptide chains. After translation and transcription, the order of the bases codes for the proteins that are made. Hope that helps!
