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

id	ftunivfreestate:oai:figshare.com:article/21713469
record_format	openpolar
spelling	ftunivfreestate:oai:figshare.com:article/21713469 2023-05-15T15:50:08+02:00 S8 Fig - Ashalatha Sreshty Mamidi (7426607) Avadhesha Surolia (78297) 2022-12-12T18:37:54Z https://doi.org/10.1371/journal.pcbi.1010661.s010 unknown https://figshare.com/articles/figure/S8_Fig_-/21713469 doi:10.1371/journal.pcbi.1010661.s010 CC BY 4.0 CC-BY 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 Image Figure 2022 ftunivfreestate https://doi.org/10.1371/journal.pcbi.1010661.s010 2022-12-16T00:32:17Z 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) Still Image Canis lupus KovsieScholar Repository (University of the Free State - UFS UV)
institution	Open Polar
collection	KovsieScholar Repository (University of the Free State - UFS UV)
op_collection_id	ftunivfreestate
language	unknown
topic	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
spellingShingle	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 Ashalatha Sreshty Mamidi (7426607) Avadhesha Surolia (78297) S8 Fig -
topic_facet	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
description	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)
format	Still Image
author	Ashalatha Sreshty Mamidi (7426607) Avadhesha Surolia (78297)
author_facet	Ashalatha Sreshty Mamidi (7426607) Avadhesha Surolia (78297)
author_sort	Ashalatha Sreshty Mamidi (7426607)
title	S8 Fig -
title_short	S8 Fig -
title_full	S8 Fig -
title_fullStr	S8 Fig -
title_full_unstemmed	S8 Fig -
title_sort	s8 fig -
publishDate	2022
url	https://doi.org/10.1371/journal.pcbi.1010661.s010
genre	Canis lupus
genre_facet	Canis lupus
op_relation	https://figshare.com/articles/figure/S8_Fig_-/21713469 doi:10.1371/journal.pcbi.1010661.s010
op_rights	CC BY 4.0
op_rightsnorm	CC-BY
op_doi	https://doi.org/10.1371/journal.pcbi.1010661.s010
_version_	1766385109186904064

S8 Fig -

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