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Residual Dipolar‐Coupling‐Based Conformational Comparison of Noncovalent Ubiquitin Homodimer with Covalently Linked Diubiquitin
Author(s) -
Shine A.,
Shenoy J.,
Jayan Parvathy,
Jiji A. C.,
Vijayan Vinesh
Publication year - 2020
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201901100
Subject(s) - dimer , covalent bond , residual dipolar coupling , chemistry , non covalent interactions , crystallography , molecule , stereochemistry , nuclear magnetic resonance spectroscopy , hydrogen bond , organic chemistry
Although the conformation of the polymer chain of Ubiquitin (Ub) mainly depends on the type of isopeptide linkage connecting two Ub molecules, the non‐covalent (noncovalent) interaction between two Ub molecules within the chain could also tune their conformational preference. Here, we studied the conformation of noncovalently formed Ub dimers in solution using residual dipolar couplings (RDCs). Comparing the RDC derived alignment tensor of the noncovalently formed dimer with the two most abundant (K11 and K48) covalent linked Ub dimers revealed that the conformation of K11 linked and noncovalent Ub dimers were similar. Between the various NMR and crystal structures of K11 linked Ub dimers, RDC tensor analysis showed that the structure of K11 linked dimer crystalized at neutral pH is similar to noncovalent dimer. Analogous to the experimental study, the comparison of predicted order matrix of various covalent Ub dimers with that of the experimentally determined order matrix of noncovalent Ub dimer also suggests that the conformation of K11 linked dimers crystalized at neutral pH is similar to the noncovalent dimer.