The PROSECCO server for chemical shift predictions in ordered and disordered proteins

Area of Science:

• Biochemistry
• Structural Biology
• Biophysics

Background:

• Nuclear Magnetic Resonance (NMR) chemical shifts provide critical insights into protein structure and dynamics.
• Correlating NMR chemical shift data with protein sequence and structure is essential for data interpretation.

Purpose of the Study:

• To present a novel sequence-based method for calculating accurate protein chemical shifts.
• To evaluate the method's performance for both ordered and disordered proteins.

Main Methods:

• Developed a sequence-based approach named protein sequences and chemical shift correlations (PROSECCO).
• Calculated chemical shifts using only protein sequence information.

Main Results:

• PROSECCO achieves accuracy comparable to advanced structure-based methods for folded proteins.
• The method significantly improves the state-of-the-art for characterizing chemical shifts in disordered proteins.
• Revealed fundamental insights into the structural information encoded in NMR chemical shifts for various protein states.

Conclusions:

• Sequence-based chemical shift prediction is feasible and accurate.
• PROSECCO offers a powerful tool for analyzing protein structure and dynamics, especially for disordered proteins.