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Nascent [Beta]-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts

Despite the important role of the unfolded states in protein stability, folding, and aggregation, they remain poorly understood due to the lack of residue-specific experimental data. Here, we explore features of the unfolded state of the NTL9 protein by applying all-atom replica-exchange simulations... Full description

Journal Title: Biophysical Journal Aug 4, 2015, p.630
Main Author: Chen, Wei
Other Authors: Shi, Chuanyin , Shen, Jana
Format: Electronic Article Electronic Article
Language: English
Subjects:
Quelle: © ProQuest LLC All rights reserved
ID: ISSN: 00063495 ; E-ISSN: 15420086
Link: http://search.proquest.com/docview/1702861331/?pq-origsite=primo
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recordid: proquest1702861331
title: Nascent [Beta]-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts
format: Article
creator:
  • Chen, Wei
  • Shi, Chuanyin
  • Shen, Jana
subjects:
  • Peptides
  • Proteins
  • Hydrogen Bonds
  • Electrostatics
ispartof: Biophysical Journal, Aug 4, 2015, p.630
description: Despite the important role of the unfolded states in protein stability, folding, and aggregation, they remain poorly understood due to the lack of residue-specific experimental data. Here, we explore features of the unfolded state of the NTL9 protein by applying all-atom replica-exchange simulations...
language: eng
source: © ProQuest LLC All rights reserved
identifier: ISSN: 00063495 ; E-ISSN: 15420086
fulltext: fulltext
issn:
  • 00063495
  • 0006-3495
  • 15420086
  • 1542-0086
url: Link


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descriptionDespite the important role of the unfolded states in protein stability, folding, and aggregation, they remain poorly understood due to the lack of residue-specific experimental data. Here, we explore features of the unfolded state of the NTL9 protein by applying all-atom replica-exchange simulations...
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titleNascent [Beta]-Hairpin Formation of a Natively Unfolded Peptide Reveals the Role of Hydrophobic Contacts
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abstractDespite the important role of the unfolded states in protein stability, folding, and aggregation, they remain poorly understood due to the lack of residue-specific experimental data. Here, we explore features of the unfolded state of the NTL9 protein by applying all-atom replica-exchange simulations...
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pubBiophysical Society
urlhttp://search.proquest.com/docview/1702861331/
date2015-08-04