The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design.

ABSTRACT: The conformational propensities of amino acids are an amalgamation of sequence effects, environmental effects and underlying intrinsic behavior. Many have attempted to investigate neighboring residue effects to aid in our understanding of protein folding and improve structure prediction efforts, especially with respect to difficult to characterize states, such as disordered or unfolded states. Host-guest peptide series are a useful tool in examining the propensities of the amino acids free from the surrounding protein structure. Here, we compare the distributions of the backbone dihedral angles (φ/ψ) of the 20 proteogenic amino acids in two different sequence contexts using the AAXAA and GGXGG host-guest pentapeptide series. We further examine their intrinsic behaviors across three environ

SUBMITTER: Childers MC 

PROVIDER: S-EPMC4917059 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature