Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water

10.12688/f1000research.2-94.v1

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Main Author: Song, J
Other Authors: BIOLOGY (NU)
Format: Article
Published: 2020
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Online Access:https://scholarbank.nus.edu.sg/handle/10635/176021
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Institution: National University of Singapore
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spelling sg-nus-scholar.10635-1760212020-09-21T04:41:58Z Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water Song, J BIOLOGY (NU) anion integral membrane protein intrinsically insoluble protein major sperm protein membrane protein protein protein SH3 sodium chloride unclassified drug vesicle associated membrane protein B vesicle associated membrane protein B3 water amino acid sequence amino terminal sequence Article binding affinity carboxy terminal sequence dynamics human nonhuman protein aggregation protein assembly protein binding protein conformation protein domain protein folding protein lipid interaction solubility 10.12688/f1000research.2-94.v1 F1000Research 2 2-94.v1 2020-09-14T07:45:28Z 2020-09-14T07:45:28Z 2013 Article Song, J (2013). Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water. F1000Research 2 : 2-94.v1. ScholarBank@NUS Repository. https://doi.org/10.12688/f1000research.2-94.v1 2046-1402 https://scholarbank.nus.edu.sg/handle/10635/176021 Unpaywall 20200831
institution National University of Singapore
building NUS Library
country Singapore
collection ScholarBank@NUS
topic anion
integral membrane protein
intrinsically insoluble protein
major sperm protein
membrane protein
protein
protein SH3
sodium chloride
unclassified drug
vesicle associated membrane protein B
vesicle associated membrane protein B3
water
amino acid sequence
amino terminal sequence
Article
binding affinity
carboxy terminal sequence
dynamics
human
nonhuman
protein aggregation
protein assembly
protein binding
protein conformation
protein domain
protein folding
protein lipid interaction
solubility
spellingShingle anion
integral membrane protein
intrinsically insoluble protein
major sperm protein
membrane protein
protein
protein SH3
sodium chloride
unclassified drug
vesicle associated membrane protein B
vesicle associated membrane protein B3
water
amino acid sequence
amino terminal sequence
Article
binding affinity
carboxy terminal sequence
dynamics
human
nonhuman
protein aggregation
protein assembly
protein binding
protein conformation
protein domain
protein folding
protein lipid interaction
solubility
Song, J
Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water
description 10.12688/f1000research.2-94.v1
author2 BIOLOGY (NU)
author_facet BIOLOGY (NU)
Song, J
format Article
author Song, J
author_sort Song, J
title Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water
title_short Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water
title_full Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water
title_fullStr Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water
title_full_unstemmed Why do proteins aggregate? "Intrinsically insoluble proteins"? And "dark mediators"? Revealed by studies on "insoluble proteins"? Solubilized in pure water
title_sort why do proteins aggregate? "intrinsically insoluble proteins"? and "dark mediators"? revealed by studies on "insoluble proteins"? solubilized in pure water
publishDate 2020
url https://scholarbank.nus.edu.sg/handle/10635/176021
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