2DUV spectroscopy can be used to monitor the local polarity of protein aromatic residues (Trp, Tyr, and Phe), which is valuable in assessing changes in protein tertiary structure since spectral properties are affected by changes in solvent exposure of these residues [17].
Biasini, M. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information.
Schneider, M., Belsom, A. & Rappsilber, J. Protein tertiary structure by crosslinking/mass spectrometry.
Biasini M, Bienert S, Waterhouse A et al. SWISS-MODEL: Modelling protein tertiary and quaternary structure using evolutionary information.
The side chains of the amino acids interact in a variety of ways to create the protein tertiary structure (hydrophobic and disulfide interactions).
Simons, K. T., Kooperberg, C., Huang, E. & Baker, D. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions.
The frequency range is associated with collective vibrational modes of protein tertiary structure.
Such factors can affect the vaccine efficacy through impacting physicochemical characteristics and protein tertiary structure.
Chemical cross-linking is a promising technology for protein tertiary structure determination.
These features are influenced by many factors, such as protein tertiary structure/confirmations, spatial distribution of the fluorescent amino acids within proteins, their side chain interactions with other residues or solvent, and resonance energy transfer among those fluorescent amino acids47,48.
