8DIJ

NMR Structure of Streptococcal Protein GB1 Backbone Modified Variant: beta-ACPC24, beta-3-Lys28, beta-3-Lys31, beta-ACPC35

Summary for 8DIJ

• Entry DOI: 10.2210/pdb8dij/pdb
• Related: 4OZB
• NMR Information: BMRB: 31031
• Descriptor: Immunoglobulin G-binding protein G (1 entity in total)
• Functional Keywords: synthetic protein, unnatural backbone, de novo protein
• Biological source: Streptococcus
• Total number of polymer chains: 1
• Total formula weight: 6246.82

Authors

Rao, S.R.,Reinert, Z.E. (deposition date: 2022-06-29, release date: 2022-11-23, Last modification date: 2023-11-15)

Primary citation

Rao, S.R.,Harmon, T.W.,Heath, S.L.,Wolfe, J.A.,Santhouse, J.R.,O'Brien, G.L.,Distefano, A.N.,Reinert, Z.E.,Horne, W.S.
Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.
Pept Sci (Hoboken), 115:-, 2023

PubMed Abstract: The construction of protein-sized synthetic chains that blend natural amino acids with artificial monomers to create so-called heterogeneous-backbones is a powerful approach to generate complex folds and functions from bio-inspired agents. A variety of techniques from structural biology commonly used to study natural proteins have been adapted to investigate folding in these entities. In NMR characterization of proteins, proton chemical shift is a straightforward to acquire, information-rich metric that bears directly on a variety of properties related to folding. Leveraging chemical shift to gain insight into folding requires a set of reference chemical shift values corresponding to each building block type (i.e., the 20 canonical amino acids in the case of natural proteins) in a random coil state and knowledge of systematic changes in chemical shift associated with particular folded conformations. Although well documented for natural proteins, these issues remain unexplored in the context of protein mimetics. Here, we report random coil chemical shift values for a library of artificial amino acid monomers frequently used to construct heterogeneous-backbone protein analogues as well as a spectroscopic signature associated with one monomer class, β-residues bearing proteinogenic side chains, adopting a helical folded conformation. Collectively, these results will facilitate the continued utilization of NMR for the study of structure and dynamics in protein-like artificial backbones.

PubMed: 37397503
DOI: 10.1002/pep2.24297

Experimental method

SOLUTION NMR