NMR reveals novel mechanisms of protein activity regulation

Charalampos Kalodimos

Research output: Contribution to journalReview article

36 Citations (Scopus)

Abstract

NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide siteresolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.

Original languageEnglish (US)
Pages (from-to)773-782
Number of pages10
JournalProtein Science
Volume20
Issue number5
DOIs
StatePublished - May 1 2011

Fingerprint

Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
Nuclear magnetic resonance spectroscopy
Entropy
Proteins
Biomolecules
Biological systems
Excited states
Conformations

Keywords

  • Allosteric interactions
  • Autoinhibition
  • NMR
  • Protein function
  • Protein regulation

Cite this

NMR reveals novel mechanisms of protein activity regulation. / Kalodimos, Charalampos.

In: Protein Science, Vol. 20, No. 5, 01.05.2011, p. 773-782.

Research output: Contribution to journalReview article

Kalodimos, Charalampos. / NMR reveals novel mechanisms of protein activity regulation. In: Protein Science. 2011 ; Vol. 20, No. 5. pp. 773-782.
@article{e9decbc8130941bfbf26c1595e7f3626,
title = "NMR reveals novel mechanisms of protein activity regulation",
abstract = "NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide siteresolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.",
keywords = "Allosteric interactions, Autoinhibition, NMR, Protein function, Protein regulation",
author = "Charalampos Kalodimos",
year = "2011",
month = "5",
day = "1",
doi = "10.1002/pro.614",
language = "English (US)",
volume = "20",
pages = "773--782",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "5",

}

TY - JOUR

T1 - NMR reveals novel mechanisms of protein activity regulation

AU - Kalodimos, Charalampos

PY - 2011/5/1

Y1 - 2011/5/1

N2 - NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide siteresolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.

AB - NMR spectroscopy is one of the most powerful tools for the characterization of biomolecular systems. A unique aspect of NMR is its capacity to provide an integrated insight into both the structure and intrinsic dynamics of biomolecules. In addition, NMR can provide siteresolved information about the conformation entropy of binding, as well as about energetically excited conformational states. Recent advances have enabled the application of NMR for the characterization of supramolecular systems. A summary of mechanisms underpinning protein activity regulation revealed by the application of NMR spectroscopy in a number of biological systems studied in the lab is provided.

KW - Allosteric interactions

KW - Autoinhibition

KW - NMR

KW - Protein function

KW - Protein regulation

UR - http://www.scopus.com/inward/record.url?scp=79954495992&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79954495992&partnerID=8YFLogxK

U2 - 10.1002/pro.614

DO - 10.1002/pro.614

M3 - Review article

VL - 20

SP - 773

EP - 782

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 5

ER -