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Amino acid's spatial positioning and the calculating of packing values both indicate the increase in the number of hydrophobic amino acids would lead to a more "tight" structure of the TR domain, which is in agreement with the trend of diminishing size of substrates transported by MCs.
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This result thus further indicates that vertebrates have a more "tight" TR structure of MCF than invertebrates.
We propose that the more "tight" TR structure generated by the increase of the hydrophobic amino acids at specific helix-helix interfaces during vertebrate evolution enhances the substrate selectivity of MCF, reflecting the evolutionary trajectory of MCF during metazoan evolution.
The more "tight" TR structure generated by the increase of the hydrophobic amino acids at specific helix-helix interfaces enhances the substrate selectivity of MCF, which reflects the evolutionary trajectory of MCF.
Further, we found that A134 was located rightly at the TRDOWN135 and evolved from S at the same site of invertebrate (Additional file 7), which indirectly supported our hypothesis that the increase of hydrophobic residues would bring in more methyl groups, further strengthening the accumulated effect of the van der Waals interaction among them and generating a more "tight" TR structure.
The optimized experimental method is capable of extending the application of the transient technique into permeability measurements of rocks with tight structure and strong gas sorption potential, providing a more reliable approach for laboratory permeability tests.
Security is more tight".
There is great freedom in having such a tight structure.
It forces you to work fast and in a tight structure.
Guys seem a little more tight".
One more tight over required now.
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