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In all, the maximum intraspecific distances are between sequences with different conformations of the inversion region, and the minimum interspecific distances occur between sequences with the same conformation.
In the water-transporting protein aquaporin a single strand with the same conformation lines one side of its water channel [ 60].
This also applies to the five GSGS folding trajectories, where each starts with the same conformation) but ends at a different conformation, 2(d) & 2 e)).
Although α-sheet with hydrogen bonds between strands is rare in native proteins in their natural state, polypeptides with the same conformation but not arranged as α-sheet do occur in some integral membrane proteins.
This structural context in subclasses IA and IB FPRs could help to explain why XacFPR, with the same conformation in its C-terminal residues as PaFPR, exhibits higher catalytic efficiency in the NADPH-diaphorase activity than RcFPR [ 4, 13] (Table S1).
The search is performed on the selected classification using BLOSUM 62 (Henikoff and Henikoff, 1992 ) as mutation table to calculate the sequence score; Classes with the same conformation and subclasses with the same geometry and/or conformation of the loops of an uploaded protein structure.
Similar(54)
Structures with compounds 2 and 3 have an asymmetric unit containing two truncated monomers, each with largely the same conformation [Cα rmsd ∼ 0.8 Å].
(B ) Cryo-NS reconstruction of the short linker dynein Lis1 complex; the linker assumes the same conformation with Lis1 bound as in the absence of Lis1.
Although modeling of single chains would suggest the possibility that those with odd number of CH2 groups adopt a flat helical shape, X-ray diffraction suggests that the chains with odd and even spacers have the same conformation, due to the necessity to pack the perylene units.
Assumptions necessary for modelling point mutations introduced through alanine-scanning mutagenesis protocol at the binding sites are that (a) they are unlikely to change the overall structure of the protein drastically and (b) the ligand moiety roughly retains the same conformation in comparison with the wild-type complex to interact with the mutated structure.
The circular dichroism (CD) spectroscopy showed that Anal R and Anal S have the same conformation of Rev NIS, with a significant fraction of helical structure.
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