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Nuclear magnetic resonance spectroscopic study was utilized to describe the solution structure and backbone dynamics of the human alpha3-chain type VI collagen. Results have shown that the global fold configuration retained its form in the solution phase and assumed the same form as in the crystal phase and C5 domain core. It was indicated that the additional six residues in the N-terminal and the 12 residues in the C-terminal affected the function of the C5 domain.

Two-dimensional NMR titration studies of the molecular properties such as hydrogen bonds, electrostatic interactions and pH-based structural modifications of Asp(B9) human insulin reveal that the Asp(B9) residue forms a B-chain alpha-helix N-cap through the helix dipole and side-chain carboxyl group interactions. All the salt bridges develop between Asn(A21) and Arg(B22) and between the Glu(B13) and His(B10) residues at an ionizing pH value. Asp(B9) is dimeric in nature and contains hydrogen bonds between the C-terminal carboxyl group of Thr(B30) residue and the amide proton of Val(A3).