Glycine in Water Favors the Polyproline II State.
glycine
molecular dynamics
protein folding
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
29 07 2020
29 07 2020
Historique:
received:
23
06
2020
revised:
22
07
2020
accepted:
27
07
2020
entrez:
6
8
2020
pubmed:
6
8
2020
medline:
10
3
2021
Statut:
epublish
Résumé
Conformational preferences of amino acid residues in water are determined by the backbone and side-chain properties. Alanine is known for its high polyproline II (pPII) propensity. The question of relative contributions of the backbone and side chain to the conformational preferences of alanine and other amino acid residues in water is not fully resolved. Because glycine lacks a heavy-atom side chain, glycine-based peptides can be used to examine to which extent the backbone properties affect the conformational space. Here, we use published spectroscopic data for the central glycine residue of cationic triglycine in water to demonstrate that its conformational space is dominated by the pPII state. We assess three commonly used molecular dynamics (MD) force fields with respect to their ability to capture the conformational preferences of the central glycine residue in triglycine. We show that pPII is the mesostate that enables the functional backbone groups of the central residue to form the most hydrogen bonds with water. Our results indicate that the pPII propensity of the central glycine in GGG is comparable to that of alanine in GAG, implying that the water-backbone hydrogen bonding is responsible for the high pPII content of these residues.
Identifiants
pubmed: 32751224
pii: biom10081121
doi: 10.3390/biom10081121
pmc: PMC7463814
pii:
doi:
Substances chimiques
Oligopeptides
0
Peptides
0
Water
059QF0KO0R
polyproline
25191-13-3
glycyl-glycyl-glycine
CVK73ZDQ8B
Glycine
TE7660XO1C
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : National Science Foundation
ID : MCB-1817650
Pays : International
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