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An octapeptide containing a central &bond;Aib–Gly– segment capable of adopting β‐turn conformations compatible with both hairpin (βII′ or βI′) and helical (βI) structures has been designed. The effect of solvent on the conformation of the peptide...
The conformational features of a chemically synthesized 23‐residue glycopeptide construct (II) carrying Gal‐β‐(1,3)‐α‐GalNAc and its deglycosylated counterpart (I; Gal: galactose; GalNAc: N‐acetyl galactosamine) derived from the C‐terminal domain of human salivary mucin (MUC7)...
We illustrate a new method for the determination of the complete binding polynomial for nucleic acids based on experimental titration data with respect to ligand concentration. From the binding polynomial, one can then calculate the distribution function for the number of ligands bound at any...
The conformational features of Pam–Lys0–Arg1–Pro2–Pro3–Gly4–Phe5–Ser6–Pro7–Phe8–Arg9–OH (PKD) and Pam–Gly−1–Lys0–Arg1–Pro2–Pro3–Gly4–Phe5–Ser6–Pro7–Phe8–Arg9–OH (PGKD), the Pam–Lys and Pam–Gly–Lys analogues of bradykinin, have been determined...
The structure of a crystalline form of Bombyx mori silk fibroin, commonly found before the spinning process (known as silk I), has been proposed as a repeated β‐turn type II‐like structure by combining data obtained from solid‐state two dimensional spin‐diffusion nuclear magnetic...
A new representation of protein sequence is devoted in this paper, in which each protein can be represented by a 20‐dimensional (20D) vector of unit length. Inspired by the principle of superposition of state in quantum mechanics, the squares of the 20 components of the vector correspond to the...
Transformations of proteins secondary and tertiary structures are generally studied in globular proteins in solution. In fibrous proteins, such as hard α‐keratin, that contain long and well‐defined double stranded α‐helical coiled coil domains, such study can be directly done on the...
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