No, protein primary structure describes linear sequence of amino acids. It doesn't covey any thing other than the sequence of amino acids, number of amino acids and number of same amino acids present. bends and coils are described in secondary as well as in tertiary structure.
To answer this question, you need to understand the structure of a peptide chain, which requires that you understand the structure of an amino acid. Simply put, amino acids consist of a nitrogen (N) atom bonded to two carbon (C) atoms: N-C-C. The middle C is bound to an 'R group'; this R group is different for each amino acid and serves to differentiate the different amino acids. The end C is bound to two oxygen (O) atoms, making it a carboxyl group. The N side is aptly called the N-terminal, and the carboxyl side is the C-terminal.
When amino acids bind to form a polypeptide chain, they link up in sequence: N-C-(C)-N-C-(C)-N-C-(C). I've put the carboxyl carbons in parentheses because they'll be important later on. Well, a long chain isn't very stable. Just as you might wind sewing thread or fishing line around a spool to get it out of the way and make sure it doesn't break, a polypeptide chain will prefer to coil up into a more stable conformation. In the simplest terms, then, the alpha helix forms because it is more stable and therefore much more favourable.
Why is it more stable? This occurs through hydrogen bonds, which form between the N's and carboxyl carbons (the carbons that I put in parentheses earlier). The helical structure happens because these hydrogen bonds form between the N of one amino acid and the C of the amino acid 4 amino acids back. In other words, if we take 1-2-3-4-5-6 to represent a chain of six amino acids, the nitrogen of amino acid #5 would form a hydrogen bond with the carboxyl carbon of amino acid #1, and same with #6 and #2. Because of how the molecular geometry and bond angles work out (the atoms involved can only form bonds at certain angles), this pattern of hydrogen bonding bends the chain into a coiled shape - a helical secondary structure.
The coils of an alpha helix or the folds of a beta-pleated sheet are a characteristic of the secondary structure.
The secondary and tertiary structures.
While it is possible to predict likely secondary structures of a protein from its primary structure, only knowing the secondary structure, the general 3-D shape of local areas of the protein, cannot yield the primary structure.
Proteins *have* primary, secondary, tertiary, and quarternary structures. The primary structure is simply the chain of amino acids without any other structure. Secondary structure results from folding of the chain to form rudimentary structures such as alpha helices, beta sheets and turns. Tertiary structure results from the further folding of the protein with secondary structures into different 3D shapes by interactions between different parts of the secondary structure. Quarternary structure results from different proteins with tertiary structures coming together to form a protein complex.
secondary, tertiary, and quaternary structures, but not primary structure
The relationship between the primary and tertiary structure of a protein is the both have a sequence of amino acids in a polypeptide chain.orThe sequence of amino acids in a primary structure determines its three-dimensional shape ( secondary and tertiary structure)
The secondary and tertiary structures.
There are four types of protein structure. These include primary structure, secondary structure, tertiary structure, and quaternary structure. Primary structure is the amino acid sequence. Secondary structure is the shape of the molecule. Tertiary structure is the interaction between groups. Quaternary structure is the interactions between protein subunits.
primary, secondary, tertiary, and quaternary
The primary structure is a one or two dimensional structure, whereas the secondary structure is a three dimensional structure in which different parts of the protein molecule bend and twist due to the formation of hydrogen bonds between atoms. This makes the secondary structure shorter than the primary structure.
The alpha helix and beta sheets are found at the Secondary level of protein folding. It's when the protein is taking its shape. Secondary structure
Quaternary tertiary secondary primary is the sequence.
There are four distinct levels of protein structure. The main two are primary, amino acid, secondary structure, and quaternary structure.
While it is possible to predict likely secondary structures of a protein from its primary structure, only knowing the secondary structure, the general 3-D shape of local areas of the protein, cannot yield the primary structure.
Proteins *have* primary, secondary, tertiary, and quarternary structures. The primary structure is simply the chain of amino acids without any other structure. Secondary structure results from folding of the chain to form rudimentary structures such as alpha helices, beta sheets and turns. Tertiary structure results from the further folding of the protein with secondary structures into different 3D shapes by interactions between different parts of the secondary structure. Quarternary structure results from different proteins with tertiary structures coming together to form a protein complex.
Primary protein structure is the order of amino acids that compose the protein and their arrangement into 2 dimensional structures like sheets or helixes is secondary. Tertiary structure is the mixed composition of secondary forms to make a three dimension protein and quaternary structure is how the protein becomes part of a functional unit like hemoglobin inside of a blood molecule.
secondary, tertiary, and quaternary structures, but not primary structure
"Helical" refers to its structure -- a helix (a spiral). See the related link below for an image.