8 citations · 8 across the 3 of their papers we have counts for
4 papers
Correlation between sequence hydrophobicity and surface-exposure pattern of database proteins
Susanne Moelbert, Eldon Emberly, Chao Tang
Hydrophobicity is thought to be one of the primary forces driving the folding of proteins. On average, hydrophobic residues occur preferentially in the core, whereas polar residues…
Flexibility of beta-sheets: Principal-component analysis of database protein structures
Eldon G. Emberly, Ranjan Mukhopadhyay, Chao Tang +1
Protein folds are built primarily from the packing together of two types of structures: alpha-helices and beta-sheets. Neither structure is rigid, and the flexibility of helices an…
Flexibility of -helices: Results of a statistical analysis of database protein structures
Eldon G. Emberly, Ranjan Mukhopadhyay, Ned S. Wingreen +1
-helices stand out as common and relatively invariant secondary structural elements of proteins. However, -helices are not rigid bodies and their deformations can be signific…
Identifying Proteins of High Designability via Surface-Exposure Patterns
Eldon G. Emberly, Jonathan Miller, Chen Zeng +2
Using an off-lattice model, we fully enumerate folded conformations of polypeptide chains of up to N = 19 monomers. Structures are found to differ markedly in designability, define…