Ribosome assisted protein folding

Some of its biological implications

Dibyendu Samanta, Anindita Das, Debasis Das, Arpita Bhattacharya, Arunima Basu, Jaydip Ghosh, Chanchal Dasgupta

Research output: Contribution to journalArticle

Abstract

One of the central characteristics of a living system is the ability to self-assemble its component molecular structures with precision and fidelity. The folding of proteins into their compact three-dimensional structures is the most fundamental and universal example of biological self-assembly. Understanding this complex process will therefore make available a unique insight into the way in which evolutionary selection has influenced the properties of a molecular system for functional advantage. The final goal of folding studies is to predict structure from sequence, allowing the design of new functional proteins and prevention of abnormal disease-associated protein conformations.

Original languageEnglish (US)
Pages (from-to)223-246
Number of pages24
JournalProteomics Research Journal
Volume1
Issue number3-4
StatePublished - 2010

Fingerprint

Protein folding
Protein Conformation
Protein Folding
Molecular Structure
Ribosomes
Proteins
Self assembly
Molecular structure
Conformations

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Cite this

Samanta, D., Das, A., Das, D., Bhattacharya, A., Basu, A., Ghosh, J., & Dasgupta, C. (2010). Ribosome assisted protein folding: Some of its biological implications. Proteomics Research Journal, 1(3-4), 223-246.

Ribosome assisted protein folding : Some of its biological implications. / Samanta, Dibyendu; Das, Anindita; Das, Debasis; Bhattacharya, Arpita; Basu, Arunima; Ghosh, Jaydip; Dasgupta, Chanchal.

In: Proteomics Research Journal, Vol. 1, No. 3-4, 2010, p. 223-246.

Research output: Contribution to journalArticle

Samanta, D, Das, A, Das, D, Bhattacharya, A, Basu, A, Ghosh, J & Dasgupta, C 2010, 'Ribosome assisted protein folding: Some of its biological implications', Proteomics Research Journal, vol. 1, no. 3-4, pp. 223-246.
Samanta D, Das A, Das D, Bhattacharya A, Basu A, Ghosh J et al. Ribosome assisted protein folding: Some of its biological implications. Proteomics Research Journal. 2010;1(3-4):223-246.
Samanta, Dibyendu ; Das, Anindita ; Das, Debasis ; Bhattacharya, Arpita ; Basu, Arunima ; Ghosh, Jaydip ; Dasgupta, Chanchal. / Ribosome assisted protein folding : Some of its biological implications. In: Proteomics Research Journal. 2010 ; Vol. 1, No. 3-4. pp. 223-246.
@article{321c0b619bfb482a9ee399854d58e087,
title = "Ribosome assisted protein folding: Some of its biological implications",
abstract = "One of the central characteristics of a living system is the ability to self-assemble its component molecular structures with precision and fidelity. The folding of proteins into their compact three-dimensional structures is the most fundamental and universal example of biological self-assembly. Understanding this complex process will therefore make available a unique insight into the way in which evolutionary selection has influenced the properties of a molecular system for functional advantage. The final goal of folding studies is to predict structure from sequence, allowing the design of new functional proteins and prevention of abnormal disease-associated protein conformations.",
author = "Dibyendu Samanta and Anindita Das and Debasis Das and Arpita Bhattacharya and Arunima Basu and Jaydip Ghosh and Chanchal Dasgupta",
year = "2010",
language = "English (US)",
volume = "1",
pages = "223--246",
journal = "Proteomics Research Journal",
issn = "1935-2824",
publisher = "Nova Science Publishers Inc",
number = "3-4",

}

TY - JOUR

T1 - Ribosome assisted protein folding

T2 - Some of its biological implications

AU - Samanta, Dibyendu

AU - Das, Anindita

AU - Das, Debasis

AU - Bhattacharya, Arpita

AU - Basu, Arunima

AU - Ghosh, Jaydip

AU - Dasgupta, Chanchal

PY - 2010

Y1 - 2010

N2 - One of the central characteristics of a living system is the ability to self-assemble its component molecular structures with precision and fidelity. The folding of proteins into their compact three-dimensional structures is the most fundamental and universal example of biological self-assembly. Understanding this complex process will therefore make available a unique insight into the way in which evolutionary selection has influenced the properties of a molecular system for functional advantage. The final goal of folding studies is to predict structure from sequence, allowing the design of new functional proteins and prevention of abnormal disease-associated protein conformations.

AB - One of the central characteristics of a living system is the ability to self-assemble its component molecular structures with precision and fidelity. The folding of proteins into their compact three-dimensional structures is the most fundamental and universal example of biological self-assembly. Understanding this complex process will therefore make available a unique insight into the way in which evolutionary selection has influenced the properties of a molecular system for functional advantage. The final goal of folding studies is to predict structure from sequence, allowing the design of new functional proteins and prevention of abnormal disease-associated protein conformations.

UR - http://www.scopus.com/inward/record.url?scp=84879828317&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84879828317&partnerID=8YFLogxK

M3 - Article

VL - 1

SP - 223

EP - 246

JO - Proteomics Research Journal

JF - Proteomics Research Journal

SN - 1935-2824

IS - 3-4

ER -