Fig 8 -

• 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.g008

Protein surface topography representing molecular hydrophobic potentials (MHP) localized to the CRD region with fourteen key residues were mapped onto 2D spherical projections for visual comparison of free and bound forms of Calnexin in Canis lupus (CNXC): (A) Free_Clus1; (B) Free_Clus2; (C) Free_Clus3; (D) Complex_Clus1; (E) Complex_Clus2; and (F) Complex_Clus1.