Ontology highlight
ABSTRACT:
SUBMITTER: Kilgore HR
PROVIDER: S-EPMC7483697 | biostudies-literature | 2020 Sep
REPOSITORIES: biostudies-literature
Kilgore Henry R HR Latham Andrew P AP Ressler Valerie T VT Zhang Bin B Raines Ronald T RT
Biochemistry 20200630 34
Glycosylation is a common modification that can endow proteins with altered physical and biological properties. Ribonuclease 1 (RNase 1), which is the human homologue of the archetypal enzyme RNase A, undergoes N-linked glycosylation at asparagine residues 34, 76, and 88. We have produced the three individual glycoforms that display the core heptasaccharide, Man<sub>5</sub>GlcNAc<sub>2</sub>, and analyzed the structure of each glycoform by using small-angle X-ray scattering along with molecular ...[more]