Macromolecule-assisted de novo protein folding

Seong Il Choi, Ahyun Son, Keo Heun Lim, Hotcherl Jeong, Baik L. Seong

Research output: Contribution to journalReview article

5 Citations (Scopus)

Abstract

In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo. Such linkage effects on the aggregation of endogenous polypeptides have been largely neglected, although all these macromolecules have been known to effectively and robustly solubilize their linked heterologous proteins in fusion or display technology. Thus, their roles in the aggregation of linked endogenous polypeptides need to be elucidated and incorporated into the mechanisms of de novo protein folding in vivo. In the classic hydrophobic interaction-based stabilizing mechanism underlying the molecular chaperone-assisted protein folding, it has been assumed that the macromolecules connected through a simple linkage without hydrophobic interactions and conformational changes would make no effect on the aggregation of their linked polypeptide chains. However, an increasing line of evidence indicates that the intrinsic properties of soluble macromolecules, especially their surface charges and excluded volume, could be important and universal factors for stabilizing their linked polypeptides against aggregation. Taken together, these macromolecules could act as folding helpers by keeping their linked nascent chains in a folding-competent state. The folding assistance provided by these macromolecules in the linkage context would give new insights into de novo protein folding inside the cell.

Original languageEnglish
Pages (from-to)10368-10386
Number of pages19
JournalInternational journal of molecular sciences
Volume13
Issue number8
DOIs
Publication statusPublished - 2012 Aug

Fingerprint

Protein folding
Protein Folding
Macromolecules
macromolecules
Polypeptides
folding
polypeptides
proteins
Peptides
Agglomeration
Hydrophobic and Hydrophilic Interactions
linkages
Proteins
Molecular Chaperones
Lipid Bilayers
Lipid bilayers
Ribosomes
Surface charge
protein synthesis
ribosomes

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

Cite this

Choi, Seong Il ; Son, Ahyun ; Lim, Keo Heun ; Jeong, Hotcherl ; Seong, Baik L. / Macromolecule-assisted de novo protein folding. In: International journal of molecular sciences. 2012 ; Vol. 13, No. 8. pp. 10368-10386.
@article{0abc34542a27433b82079c5064f4ee50,
title = "Macromolecule-assisted de novo protein folding",
abstract = "In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo. Such linkage effects on the aggregation of endogenous polypeptides have been largely neglected, although all these macromolecules have been known to effectively and robustly solubilize their linked heterologous proteins in fusion or display technology. Thus, their roles in the aggregation of linked endogenous polypeptides need to be elucidated and incorporated into the mechanisms of de novo protein folding in vivo. In the classic hydrophobic interaction-based stabilizing mechanism underlying the molecular chaperone-assisted protein folding, it has been assumed that the macromolecules connected through a simple linkage without hydrophobic interactions and conformational changes would make no effect on the aggregation of their linked polypeptide chains. However, an increasing line of evidence indicates that the intrinsic properties of soluble macromolecules, especially their surface charges and excluded volume, could be important and universal factors for stabilizing their linked polypeptides against aggregation. Taken together, these macromolecules could act as folding helpers by keeping their linked nascent chains in a folding-competent state. The folding assistance provided by these macromolecules in the linkage context would give new insights into de novo protein folding inside the cell.",
author = "Choi, {Seong Il} and Ahyun Son and Lim, {Keo Heun} and Hotcherl Jeong and Seong, {Baik L.}",
year = "2012",
month = "8",
doi = "10.3390/ijms130810368",
language = "English",
volume = "13",
pages = "10368--10386",
journal = "International Journal of Molecular Sciences",
issn = "1661-6596",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "8",

}

Macromolecule-assisted de novo protein folding. / Choi, Seong Il; Son, Ahyun; Lim, Keo Heun; Jeong, Hotcherl; Seong, Baik L.

In: International journal of molecular sciences, Vol. 13, No. 8, 08.2012, p. 10368-10386.

Research output: Contribution to journalReview article

TY - JOUR

T1 - Macromolecule-assisted de novo protein folding

AU - Choi, Seong Il

AU - Son, Ahyun

AU - Lim, Keo Heun

AU - Jeong, Hotcherl

AU - Seong, Baik L.

PY - 2012/8

Y1 - 2012/8

N2 - In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo. Such linkage effects on the aggregation of endogenous polypeptides have been largely neglected, although all these macromolecules have been known to effectively and robustly solubilize their linked heterologous proteins in fusion or display technology. Thus, their roles in the aggregation of linked endogenous polypeptides need to be elucidated and incorporated into the mechanisms of de novo protein folding in vivo. In the classic hydrophobic interaction-based stabilizing mechanism underlying the molecular chaperone-assisted protein folding, it has been assumed that the macromolecules connected through a simple linkage without hydrophobic interactions and conformational changes would make no effect on the aggregation of their linked polypeptide chains. However, an increasing line of evidence indicates that the intrinsic properties of soluble macromolecules, especially their surface charges and excluded volume, could be important and universal factors for stabilizing their linked polypeptides against aggregation. Taken together, these macromolecules could act as folding helpers by keeping their linked nascent chains in a folding-competent state. The folding assistance provided by these macromolecules in the linkage context would give new insights into de novo protein folding inside the cell.

AB - In the processes of protein synthesis and folding, newly synthesized polypeptides are tightly connected to the macromolecules, such as ribosomes, lipid bilayers, or cotranslationally folded domains in multidomain proteins, representing a hallmark of de novo protein folding environments in vivo. Such linkage effects on the aggregation of endogenous polypeptides have been largely neglected, although all these macromolecules have been known to effectively and robustly solubilize their linked heterologous proteins in fusion or display technology. Thus, their roles in the aggregation of linked endogenous polypeptides need to be elucidated and incorporated into the mechanisms of de novo protein folding in vivo. In the classic hydrophobic interaction-based stabilizing mechanism underlying the molecular chaperone-assisted protein folding, it has been assumed that the macromolecules connected through a simple linkage without hydrophobic interactions and conformational changes would make no effect on the aggregation of their linked polypeptide chains. However, an increasing line of evidence indicates that the intrinsic properties of soluble macromolecules, especially their surface charges and excluded volume, could be important and universal factors for stabilizing their linked polypeptides against aggregation. Taken together, these macromolecules could act as folding helpers by keeping their linked nascent chains in a folding-competent state. The folding assistance provided by these macromolecules in the linkage context would give new insights into de novo protein folding inside the cell.

UR - http://www.scopus.com/inward/record.url?scp=84878638259&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84878638259&partnerID=8YFLogxK

U2 - 10.3390/ijms130810368

DO - 10.3390/ijms130810368

M3 - Review article

C2 - 22949867

AN - SCOPUS:84878638259

VL - 13

SP - 10368

EP - 10386

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1661-6596

IS - 8

ER -