Search: onr:"swepub:oai:DiVA.org:kth-285646" >
Glutenin and Gliadi...
Glutenin and Gliadin, a Piece in the Puzzle of their Structural Properties in the Cell Described through Monte Carlo Simulations
-
- Markgren, Joel (author)
- Sveriges lantbruksuniversitet,Swedish University of Agricultural Sciences,Institutionen för växtförädling,Department of Plant Breeding
-
- Hedenqvist, Mikael S. (author)
- KTH Royal Institute of Technology,KTH,Fiber- och polymerteknologi
-
- Rasheed, Faiza (author)
- KTH Royal Institute of Technology,KTH,Polymera material
-
show more...
-
- Skepö, Marie (author)
- Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
-
- Johansson, Eva (author)
- Sveriges lantbruksuniversitet,Swedish University of Agricultural Sciences,Institutionen för växtförädling,Department of Plant Breeding
-
show less...
-
(creator_code:org_t)
-
- 2020-07-23
- 2020
- English.
-
In: Biomolecules. - : MDPI. - 2218-273X. ; 10:8
- Related links:
-
https://doi.org/10.3...
-
show more...
-
https://www.mdpi.com...
-
http://dx.doi.org/10... (free)
-
https://pub.epsilon.... (primary) (Raw object) (free)
-
https://urn.kb.se/re...
-
https://doi.org/10.3...
-
https://lup.lub.lu.s...
-
https://res.slu.se/i...
-
show less...
Abstract
Subject headings
Close
- Gluten protein crosslinking is a predetermined process where specific intra- and intermolecular disulfide bonds differ depending on the protein and cysteine motif. In this article, all-atom Monte Carlo simulations were used to understand the formation of disulfide bonds in gliadins and low molecular weight glutenin subunits (LMW-GS). The two intrinsically disordered proteins appeared to contain mostly turns and loops and showed "self-avoiding walk" behavior in water. Cysteine residues involved in intramolecular disulfide bonds were located next to hydrophobic peptide sections in the primary sequence. Hydrophobicity of neighboring peptide sections, synthesis chronology, and amino acid chain flexibility were identified as important factors in securing the specificity of intramolecular disulfide bonds formed directly after synthesis. The two LMW-GS cysteine residues that form intermolecular disulfide bonds were positioned next to peptide sections of lower hydrophobicity, and these cysteine residues are more exposed to the cytosolic conditions, which influence the crosslinking behavior. In addition, coarse-grained Monte Carlo simulations revealed that the protein folding is independent of ionic strength. The potential molecular behavior associated with disulfide bonds, as reported here, increases the biological understanding of seed storage protein function and provides opportunities to tailor their functional properties for different applications.
Subject headings
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- modeling
- intrinsically disordered proteins
- gluten
- disulfide bonds
- cysteine
- prolamin
- Monte Carlo
- Cysteine
- Disulfide bonds
- Gluten
- Intrinsically disordered proteins
- Modeling
- Monte Carlo
- Prolamin
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database