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This 'globin fold' typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini. [4] Since the globin fold contains only helices, it is classified as an all-alpha protein fold. The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold was thus the ...
In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies (i.e. are not necessarily evolutionarily related to one another). [1] [2] [3]
There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold. [2]
Globin superfamily Members share an 8-alpha helix globular globin fold. [28] [29] Immunoglobulin superfamily Members share a sandwich-like structure of two sheets of antiparallel β strands , and are involved in recognition, binding, and adhesion. [30] [31] PA clan
For example, the "globin-like" fold is described as core: 6 helices; folded leaf, partly opened. The fold to which a domain belongs is determined by inspection, rather than by software. The levels of SCOP version 1.75 are as follows. Class: Types of folds, e.g., beta sheets. Fold: The different shapes of domains within a class.
Each protein chain arranges into a set of alpha-helix structural segments connected together in a globin fold arrangement. Such a name is given because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin. [45] [46] This folding pattern contains a pocket that strongly binds the heme group. [citation ...
Two types of the globin fold have been identified in Phytogbs: the 3/3- and 2/2-folding, [9] [10] where helices A, E and F overlap to helices B, G and H and helices B and E overlap to helices G and H, respectively. Like other globins, heme-Fe in Phytogbs is coordinated at the proximal region by a His amino acid (named as proximal His).
Proteins typically fold within 0.1 and 1000 seconds. Therefore, the protein folding process must be directed some way through a specific folding pathway. The forces that direct this search are likely to be a combination of local and global influences whose effects are felt at various stages of the reaction. [53]