schliessen

Filtern

 

Bibliotheken

Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein (Engineering Short AFPs from a Globular Folded AFP)

Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group... Full description

Journal Title: 2012 Vol.7(11), p.e49788
Main Author: Shah, Syed Hussinien H
Other Authors: Kar, Rajiv K , Asmawi, Azren A , Rahman, Mohd Basyaruddin A , Murad, Abdul Munir A , Mahadi, Nor M , Basri, Mahiran , Rahman, Raja Noor Zaliha A , Salleh, Abu B , Chatterjee, Subhrangsu , Tejo, Bimo A , Bhunia, Anirban
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0049788
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: plos10.1371/journal.pone.0049788
title: Solution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein (Engineering Short AFPs from a Globular Folded AFP)
format: Article
creator:
  • Shah, Syed Hussinien H
  • Kar, Rajiv K
  • Asmawi, Azren A
  • Rahman, Mohd Basyaruddin A
  • Murad, Abdul Munir A
  • Mahadi, Nor M
  • Basri, Mahiran
  • Rahman, Raja Noor Zaliha A
  • Salleh, Abu B
  • Chatterjee, Subhrangsu
  • Tejo, Bimo A
  • Bhunia, Anirban
subjects:
  • Research Article
  • Biology
  • Chemistry
  • Chemistry
  • Computational Biology
  • Biophysics
  • Biochemistry
ispartof: 2012, Vol.7(11), p.e49788
description: Exotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities.
language: eng
source:
identifier: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0049788
fulltext: fulltext
issn:
  • 1932-6203
  • 19326203
url: Link


@attributes
ID829239466
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid10.1371/journal.pone.0049788
sourceidplos
recordidTN_plos10.1371/journal.pone.0049788
sourcesystemOther
pqid1350901862
galeid477008450
display
typearticle
titleSolution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein (Engineering Short AFPs from a Globular Folded AFP)
creatorShah, Syed Hussinien H ; Kar, Rajiv K ; Asmawi, Azren A ; Rahman, Mohd Basyaruddin A ; Murad, Abdul Munir A ; Mahadi, Nor M ; Basri, Mahiran ; Rahman, Raja Noor Zaliha A ; Salleh, Abu B ; Chatterjee, Subhrangsu ; Tejo, Bimo A ; Bhunia, Anirban
contributorMassiah, Michael (Editor)
ispartof2012, Vol.7(11), p.e49788
identifierE-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0049788
subjectResearch Article ; Biology ; Chemistry ; Chemistry ; Computational Biology ; Biophysics ; Biochemistry
descriptionExotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities.
languageeng
source
version9
lds50peer_reviewed
links
openurl$$Topenurl_article
openurlfulltext$$Topenurlfull_article
search
creatorcontrib
0Shah, Syed Hussinien H
1Kar, Rajiv K
2Asmawi, Azren A
3Rahman, Mohd Basyaruddin A
4Murad, Abdul Munir A
5Mahadi, Nor M
6Basri, Mahiran
7Rahman, Raja Noor Zaliha A
8Salleh, Abu B
9Chatterjee, Subhrangsu
10Tejo, Bimo A
11Bhunia, Anirban
12Massiah, Michael (Editor)
titleSolution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein (Engineering Short AFPs from a Globular Folded AFP)
descriptionExotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities.
subject
0Research Article
1Biology
2Chemistry
3Computational Biology
4Biophysics
5Biochemistry
general
010.1371/journal.pone.0049788
1English
sourceidplos
recordidplos10.1371/journal.pone.0049788
issn
01932-6203
119326203
rsrctypearticle
creationdate2012
recordtypearticle
addtitleEngineering Short AFPs from a Globular Folded AFP
searchscopeplos
scopeplos
lsr30VSR-Enriched:[pqid, galeid]
sort
titleSolution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein (Engineering Short AFPs from a Globular Folded AFP)
authorShah, Syed Hussinien H ; Kar, Rajiv K ; Asmawi, Azren A ; Rahman, Mohd Basyaruddin A ; Murad, Abdul Munir A ; Mahadi, Nor M ; Basri, Mahiran ; Rahman, Raja Noor Zaliha A ; Salleh, Abu B ; Chatterjee, Subhrangsu ; Tejo, Bimo A ; Bhunia, Anirban
creationdate20121128
facets
frbrgroupid6776627556871509995
frbrtype5
languageeng
creationdate2012
topic
0Research Article
1Biology
2Chemistry
3Computational Biology
4Biophysics
5Biochemistry
collectionPLoS
prefilterarticles
rsrctypearticles
creatorcontrib
0Shah, Syed Hussinien H
1Kar, Rajiv K
2Asmawi, Azren A
3Rahman, Mohd Basyaruddin A
4Murad, Abdul Munir A
5Mahadi, Nor M
6Basri, Mahiran
7Rahman, Raja Noor Zaliha A
8Salleh, Abu B
9Chatterjee, Subhrangsu
10Tejo, Bimo A
11Bhunia, Anirban
12Massiah, Michael
toplevelpeer_reviewed
frbr
t2
k12012
k219326203
k310.1371/journal.pone.0049788
k47
k511
k649788
k8solution structures dynamics ice growth inhibitory activity of peptide fragments derived from an antarctic yeast protein
k9solutionstructuresdyotein
k12solutionstructuresdynamic
k15syedhussinienhshah
k16shahsyedhussinienh
delivery
delcategoryRemote Search Resource
fulltextfulltext
ranking
booster11
booster21
pcg_typepublisher
addata
aulast
0Shah
1Kar
2Asmawi
3Rahman
4Murad
5Mahadi
6Basri
7Salleh
8Chatterjee
9Tejo
10Bhunia
11Massiah
aufirst
0Syed Hussinien H.
1Rajiv K.
2Azren A.
3Mohd Basyaruddin A.
4Abdul Munir A.
5Nor M.
6Mahiran
7Raja Noor Zaliha A.
8Abu B.
9Subhrangsu
10Bimo A.
11Anirban
12Michael
au
0Shah, Syed Hussinien H
1Kar, Rajiv K
2Asmawi, Azren A
3Rahman, Mohd Basyaruddin A
4Murad, Abdul Munir A
5Mahadi, Nor M
6Basri, Mahiran
7Rahman, Raja Noor Zaliha A
8Salleh, Abu B
9Chatterjee, Subhrangsu
10Tejo, Bimo A
11Bhunia, Anirban
addauMassiah, Michael
atitleSolution Structures, Dynamics, and Ice Growth Inhibitory Activity of Peptide Fragments Derived from an Antarctic Yeast Protein (Engineering Short AFPs from a Globular Folded AFP)
risdate20121128
volume7
issue11
spagee49788
pagese49788
eissn1932-6203
genrearticle
ristypeJOUR
abstractExotic functions of antifreeze proteins (AFP) and antifreeze glycopeptides (AFGP) have recently been attracted with much interest to develop them as commercial products. AFPs and AFGPs inhibit ice crystal growth by lowering the water freezing point without changing the water melting point. Our group isolated the Antarctic yeast Glaciozyma antarctica that expresses antifreeze protein to assist it in its survival mechanism at sub-zero temperatures. The protein is unique and novel, indicated by its low sequence homology compared to those of other AFPs. We explore the structure-function relationship of G. antarctica AFP using various approaches ranging from protein structure prediction, peptide design and antifreeze activity assays, nuclear magnetic resonance (NMR) studies and molecular dynamics simulation. The predicted secondary structure of G. antarctica AFP shows several α-helices, assumed to be responsible for its antifreeze activity. We designed several peptide fragments derived from the amino acid sequences of α-helical regions of the parent AFP and they also showed substantial antifreeze activities, below that of the original AFP. The relationship between peptide structure and activity was explored by NMR spectroscopy and molecular dynamics simulation. NMR results show that the antifreeze activity of the peptides correlates with their helicity and geometrical straightforwardness. Furthermore, molecular dynamics simulation also suggests that the activity of the designed peptides can be explained in terms of the structural rigidity/flexibility, i.e., the most active peptide demonstrates higher structural stability, lower flexibility than that of the other peptides with lower activities, and of lower rigidity. This report represents the first detailed report of downsizing a yeast AFP into its peptide fragments with measurable antifreeze activities.
copSan Francisco, USA
pubPublic Library of Science
doi10.1371/journal.pone.0049788
oafree_for_read
date2012-11-28