Parallel beta sheets are less stable than anti-parallel beta sheets because of the weaker hydrogen bonding interactions between strands in parallel sheets. The alignment of hydrogen bond donors and acceptors in parallel beta sheets reduces the strength of hydrogen bonds, leading to lower stability. In anti-parallel beta sheets, the hydrogen bonds are more linear and therefore stronger, enhancing the overall stability of the structure.
Proteins are the type of macromolecules made of amino acids. Each protein is a chain of amino acids folded into a specific three-dimensional structure that determines its function.
The secondary structure of protein:the ordered 3-d arrangements in localized area of a polypeptide chaininteractions of the peptide backbone (s-trans and planar)example of secondary structure : alpha-helix and beta-pleated sheet
The atoms present in a protein molecule are bonded to each other by covalent bonds. Added: I think the questioner wants...., A special amide bond called a peptide bond binds the amino acid subunits together and in a folded protein you will get hydrogen bonds, hydrophyllic bonding, hydrophobic bonding and covalent sulfur-sulfur bonding to name several types.
When a globular protein has its hydrogen bonds broken, it can become denatured. This disrupts its folded structure, causing it to lose its specific shape and potentially its function. This could be reversible or irreversible depending on the extent of damage to the protein.
The term used to describe the arrangement of different polypeptide chains in a protein is "quaternary structure." This structure refers to the spatial arrangement of multiple folded protein subunits held together by non-covalent interactions, forming a functional protein complex.
hydrogen bonds
Biomolecular structure is the intricate folded, three-dimensional shape that is formed by a molecule of protein, DNA, or RNA, and that is important to its function.
The DNA sequence will determine the amino acid sequence known as the protein's primary structure. As the protein is folded into the secondary, tertiary and quatranary structures, the amino acid molecules will determine the shape
The DNA sequence will determine the amino acid sequence known as the protein's primary structure. As the protein is folded into the secondary, tertiary and quatranary structures, the amino acid molecules will determine the shape
A prion is a misfolded form of a protein molecule, specifically the prion protein (PrP). It can induce other normally folded PrP proteins to adopt the misfolded conformation, leading to the spread of prion diseases.
When a polypeptide is folded into its three-dimensional structure, it is referred to as a protein. Proteins are made up of one or more polypeptide chains that have folded into a specific conformation to perform their biological functions.
The triplet of bases at one end of a folded tRNA molecule is called the anticodon. This anticodon base-pairs with a complementary sequence of three bases, called the codon, in mRNA during protein synthesis. This specific interaction ensures the accurate incorporation of the correct amino acid into the growing polypeptide chain.
Parallel belts of folded mountains and volcanic mountains
An enzyme is a folded protein. When this folded protein becomes denatured, it essentially stops working. It can not function due to high temperatures or wrong pH.
Protein production involves transcription, where DNA is used as a template to make mRNA. This mRNA is then translated by ribosomes to assemble amino acids into a protein molecule according to the genetic code. Finally, the protein is folded into its functional form and may undergo post-translational modifications.
A protein is a complex molecule made up of chains of amino acids folded into a specific shape. Its structure is defined by the sequence of amino acids and how they interact with each other through various bonds and interactions. This unique structure determines the protein's function in the body.
The native fold refers to the specific three-dimensional shape a protein molecule adopts when it is functioning properly in a biological system. This folded structure is essential for the protein to carry out its biological functions effectively. Any deviation from the native fold can lead to protein misfolding and potential loss of function or disease.