me:)
nah its just a joke
sorry i dont know these im in yr y11 4 gods sake
plz forgive me:)
Primary- Covalent bonds Secondary- Hydrogen bonds Tertiary- Hydrophobic interactions - Disulphide bonds/bridges - Hydrogen bonding Quaternary- (Same as Tertiary)
Quaternary structure. This structure results from the assembly of multiple polypeptide chains to form a functional protein complex. The individual chains in the complex can interact through various types of bonds, such as hydrogen bonds, disulfide bonds, and hydrophobic interactions.
Saturated fats have carbon-hydrogen chains with single bonds between carbon atoms. Unsaturated fats have carbon-carbon double bonds, leading to kinks in the carbon-hydrogen chains.
hydrogen bonds, disulphide bonds
Interchain hydrogen bonds form between different protein chains, such as in a multimeric protein complex. Intrachain hydrogen bonds form within the same protein chain, stabilizing the secondary structure, such as alpha helices or beta sheets. Both types of hydrogen bonds contribute to the overall stability and structure of proteins.
It is a protein They have both quartenary structures haemogalobin has 4 polypeptide chains with a prosthetic heam group and Collagen 3 polypeptide chains wound around each other by hydrogen bonds.
Hydrogen Bonds
If a protein's hydrogen bonds are broken, its structure may be disrupted, leading to a loss of function. Hydrogen bonds are important for maintaining the specific shape and stability of proteins, and any disruption in these bonds can alter the protein's ability to bind to other molecules or carry out its biological function.
the protein's structure through the alteration of its hydrogen bonding patterns. Acids can cause protonation of amino acid side chains, while bases can cause deprotonation. These chemical changes can lead to unfolding of the protein and loss of its function.
Hydrogen bonds stabilize the secondary structure of proteins, such as alpha helices and beta sheets, by forming between the backbone amide groups. They also help in maintaining the tertiary structure by forming between side chains of amino acids to hold the protein in its functional 3D shape. Hydrogen bonds play a crucial role in protein folding and maintaining overall stability.
Protein molecules have covalent bonds in them, and there are hydrogen bonds that act as intermolecular bonds.
The weak electrical attractions within polypeptide chains, such as hydrogen bonds and van der Waals interactions, contribute to the folding of the protein into its specific three-dimensional structure. These interactions help stabilize the protein's conformation and are crucial for its function and stability.