High impact information on VMO1

• A new protein fold with internal symmetry has been observed in two proteins: vitelline membrane outer layer protein I (VMO-I) and delta-endotoxin [1].
• The outer layer of the vitelline membrane from hen egg yolk consists of ovomucin, vitelline membrane outer layer protein I (VMOI) and lysozyme [2].
• Sixteen proteins were identified, and among them, two had never been previously detected in hen egg white, i.e., Tenp, a protein with strong homology with a bacterial permeability-increasing protein family (BPI), and VMO-1, an outer layer vitelline membrane protein [3].

Biological context of VMO1

• Characterization of vitelline membrane outer layer protein I, VMO-I: amino acid sequence and structural stability [4].

Anatomical context of VMO1

• Vitelline membrane outer layer protein I (VMO-I) tightly bound to ovomucin fibrils of hen's egg yolk membrane was characterized in terms of its amino acid sequence and structural stability [4].

Analytical, diagnostic and therapeutic context of VMO1

• The sequence analyses show that VMO-I contains three 53-residue internal repeats that contain distinctive regions of turns flanked by beta-sheets consistent with the recent finding that the molecule contains a new beta-fold motif, the beta-prism [4].
• The molecular characteristics of VMO-I in solution were examined by CD spectroscopy in the far and near ultraviolet regions, NMR spectroscopy, and high sensitive differential scanning calorimetry (DSC) [4].
• Crystallization and preliminary crystallographic data of vitelline membrane outer layer protein I, VMO-I [5].

References