S8 Fig -

Plots showing radius of gyration (Rg) computed as a function of time for Calnexin group of lectins in free form: (A) Calnexin in Canis lupus (CNXC); (B) Calnexin in humans (CNXH); and (C) Calmegin (CLMG). (TIF)

Bibliographic Details
Main Authors:	Ashalatha Sreshty Mamidi (7426607), Avadhesha Surolia (78297)
Format:	Still Image
Language:	unknown
Published:	2022
Subjects:	Biophysics Biochemistry Cell Biology Genetics Molecular Biology Evolutionary Biology Cancer Computational Biology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified two competing theories similar structural architectures several conformations spanning reducing end glucose provide valuable insight conserved functional roles explain biomolecular recognition carbohydrate recognition domain protein folding process noncovalent bond interactions molecular interaction fields bound forms demonstrated central mannose residues molecular recognition process conformational selection followed proteins </ p favorable lectin conformation molecular recognition conformational selection specific interactions protein sequence also demonstrated trp residues key residues conformational changes xlink "> since exploring scientific scrutiny molecular structure mmpbsa approach ligand binding initially driven induced fluctuations induced fit hydrophobic potentials fundamental question atomistic simulations &# 8220 Canis lupus
Online Access:	https://doi.org/10.1371/journal.pcbi.1010661.s010

Description
Summary:	Plots showing radius of gyration (Rg) computed as a function of time for Calnexin group of lectins in free form: (A) Calnexin in Canis lupus (CNXC); (B) Calnexin in humans (CNXH); and (C) Calmegin (CLMG). (TIF)