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In the autoinhibited conformation, vinculin is unable to interact with binding partners due to intramolecular interactions between Vt and Vh.
It is determined only by intramolecular interactions.
However, the surface of folded subdomains is generally polar resulting in low affinity intramolecular interactions.
Residues involved in intramolecular interactions, also shown in (B D), are highlighted.
Intramolecular interactions within the primary amino acid sequence drives polypeptides to fold.
Various intramolecular interactions were analysed by AIM approach.
Weak intramolecular interactions were found using AIM analyses.
The partial X-ray structure of RNF125 revealed the presence of extensive intramolecular interactions between the RING and C2HC ZnF.
For the folding of multidomain proteins, the subdomains act as the primary sequence and their intramolecular interactions drive supertertiary folding.
Interestingly, the structure demonstrates that extensive intramolecular interactions take place between the RING domain and the C2HC ZnF (Fig. 7A).
Weak intramolecular interactions permit a dynamic ensemble of alternate conformations, which is difficult to predict and challenging to identify experimentally.
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