The hydrogen bonds between adjacent peptide linkages in a protein that stabalize the structure of the protein.
Regular local folding pattern of a polymeric molecule; in proteins, helices and -pleated sheets.
The conformation of a protein created by the formation of hydrogen bonds between different amino acids; can be a pleated sheet (beta sheet), alpha helix, or random coil.
Those regular elements of two-dimensional structure common to many proteins that are formed by relatively short-range interactions within the polypeptide chain. Examples are Î±-helix and Î²-pleated sheet.
In proteins, local folding of a polypeptide chain into regular structures including the ¥á helix, ¥â pleated sheet, and U-shaped turns and loops.
Level of structural organization in proteins described by the folding of the polypeptide chain into structural motifs such as alpha helices and beta sheets, which involve hydrogen bonding of backbone atoms. Secondary structure is also formed in nucleic acids, especially in single-stranded RNA's by internal base pairing
The alpha-helical or beta-sheet configuration of the polypeptide backbone of a protein.
The level of protein substructuret that involves organization of chain sections into ordered arrangements such as B-pleated sheets or a-helices.
In proteins and nucleic acids, the structure of the molecule brought about by the formation of hydrogen bonds between amino acids or nucleotides, respectively. In proteins, the localized structures in the polypeptide chain (e.g., a-helix, §-sheet, turn). In single-stranded DNA or RNA, the localized double-stranded structures (e.g., hairpins).
Of a protein, localized regularities of structure, such as the a helix and the b pleated sheet.
the three-dimensional structure of the protein chain (for example, a-helix, random coil, or pleated sheet)
The initial intramolecular interactions that occur as a protein begins to fold. Examples of these interactions are hydrogen bonding between different amino acid residues or the disulfide bonds that form between the sulfur moieties of two individual cysteine residues. See also Conformation, Primary Structure, Quaternary Structure, Tertiary Structure.
a repeating three-dimensional structure with a fixed bonding pattern
Regions of local regularity within a protein fold (e.g., ¦Á-helices, ¦Â-turns, ¦Â-strands.).
The arrangement of a protein chain into regular hydrogen-bonded structures such as a helix or b sheet.
The structure of a protein created by the formation of hydrogen bonds between different amino acids; can be a pleated sheet, alpha helix, or random coil. Shape of a protein caused by attraction between R-groups of amino acids. PICTURE
The collection of contiguous peptide segments with repetitive values for and . Each segment may be -helix or -sheet. Proteins are classified according to the types and arrangements of their peptide segments. Secondary structure tends to be conserved among related proteins.
the first level of actual folding of the backbone of a linear polymer to form a regular, repeating structure. Examples are the B- and Z-helical forms of DNA and the alpha-helix and beta-sheet structures of polypeptides.
Localized three dimensional structure of the protein molecule caused by (generally) short range interaction between amino acids in the protein; examples of secondary structure include beta pleated sheets and alpha helix.
A three dimensional form of different segments of a protein that does not define specific atomic positions.
For proteins refers to that aspect of a proteins three dimensional structure which is due to the geometry of amino acid bonding between adjacent amino acids and short range hydrogen bonding. Typical secondary structures are pleated plates and alpha helices.
Certain highly regular three-dimensional arrangements of amino acids within a protein.
Secondary structure in biochemistry and structural biology describes the general three-dimensional form of local segments of biopolymers such as proteins and nucleic acids (DNA/RNA). It does not, however, describe specific atomic positions in three-dimensional space, which are considered to be tertiary structure.