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The Dictionary of Protein Secondary Structure, in short DSSP, is commonly used to describe the protein secondary structure with single letter codes. The secondary structure is assigned based on hydrogen bonding patterns as those initially proposed by Pauling et al. in 1951 (before any protein structure had ever been experimentally determined).
A membrane transport protein is a membrane protein involved in the movement of ions, small molecules, and macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins ; that is they exist permanently within and span the membrane across which they transport substances.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids , which are the monomers of the polymer.
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 structure of these molecules may be considered at any of several length scales ranging from the level of individual atoms to the relationships among entire protein subunits.
Schematic representation of transmembrane proteins: 1) a single-pass membrane protein 2) a multipass membrane protein (α-helix) 3) a multipass membrane protein β-sheet. The membrane is represented in light yellow. A transmembrane protein is a type of integral membrane protein that spans the entirety of the cell membrane.
The words protein, polypeptide, and peptide are a little ambiguous and can overlap in meaning. Protein is generally used to refer to the complete biological molecule in a stable conformation, whereas peptide is generally reserved for a short amino acid oligomers often lacking a stable 3D structure. But the boundary between the two is not well ...
The rate of ion transport through the channel is very high (often 10 6 ions per second or greater). Ions pass through channels down their electrochemical gradient , which is a function of ion concentration and membrane potential, "downhill", without the input (or help) of metabolic energy (e.g. ATP , co-transport mechanisms, or active transport ...
This phenomenon, where molecule Y affects the binding of molecule X to a transport molecule Z, is called a heterotropic allosteric effect. Hemoglobin in organisms at high altitudes has also adapted such that it has less of an affinity for 2,3-BPG and so the protein will be shifted more towards its R state.