Context is a major determinant of beta-sheet propensity.
Abstract
Residues in beta-sheets occur in two distinct tertiary contexts: central strands, bordered on both sides by other beta-strands, and edge strands, bordered on only a single side by another beta-strand. The delta delta G values for beta-sheet formation measured at an edge beta-strand of the IgG-binding domain of protein G(GB1) are quite different from those obtained previously at a central position in the same protein. In particular, there is no correlation at the edge position with statistically determined beta-sheet-forming preferences. The differences between beta-sheet propensities measured at central and edge beta-strands, delta delta delta G values, correlate with the values of water/octanol transfer free energies and side-chain non-polar surface area for the amino acids. These results strongly suggest that, unlike alpha-helix formation, beta-sheet formation is determined in large part by tertiary context, even at solvent-accessible sites, and not by intrinsic secondary structure preferences.
Submission Details
ID: n2LZ8GcT
Submitter: Connie Wang
Submission Date: Nov. 7, 2017, 9:31 p.m.
Version: 3
Publication Details
Minor DL Jr;Kim PS,Nature (1994) Context is a major determinant of beta-sheet propensity. PMID:8078589Additional Information
Study Summary
| Number of data points | 58 |
| Proteins | Immunoglobulin G-binding protein G |
| Unique complexes | 20 |
| Assays/Quantities/Protocols | Experimental Assay: Ka/KaAAA-44Thr -- Relative binding constant to human Fc AAA-44Thr ; Experimental Assay: ∆∆G (relative to alanine) ; Experimental Assay: Tm |
| Libraries | Parameters of beta-sheet formation |
Structure view and single mutant data analysis
Study data
| Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Data Distribution
Studies with similar sequences (approximate matches)