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Myoglobin sketch Alpha helix. 1958 – Myoglobin was the very first crystal structure of a protein molecule. [2] Myoglobin cradles an iron-containing heme group that reversibly binds oxygen for use in powering muscle fibers, and those first crystals were of myoglobin from the sperm whale, whose muscles need copious oxygen storage for deep dives.
A protein contact map represents the distance between all possible amino acid residue pairs of a three-dimensional protein structure using a binary two-dimensional matrix. For two residues i {\displaystyle i} and j {\displaystyle j} , the i j {\displaystyle ij} element of the matrix is 1 if the two residues are closer than a predetermined ...
[10] [11] [13] The Cr-O bond length ranges from 1.949 to 1.957 Å. [12] The crystal structure has only been recently described in 2013. [ 13 ] Water does not coordinate to the Cr 3+ center and is instead thought to hydrogen bond between other Cr(Pic) 3 complexes to form a network of Cr(Pic) 3 complexes.
According to one definition, a turn is a structural motif where the C α atoms of two residues separated by a few (usually 1 to 5) peptide bonds are close (less than 7 Å [0.70 nm]). [1] The proximity of the terminal C α atoms often correlates with formation of an inter main chain hydrogen bond between the corresponding residues.
A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins.
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. [1] [2] A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains [3] although there may be up to 3000 human zinc metalloproteins. [4]
Although the active site occupies only ~10–20% of the volume of an enzyme, [1]: 19 it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes. [2]
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).