Structure. 2009 Sep 9;17(9):1169-85.

Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.

Jensen MR, Markwick PR, Meier S, Griesinger C, Zweckstetter M, Grzesiek S, Bernadó P, Blackledge M.

Source

Protein Dynamics and Flexibility, Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, Grenoble, France.

Abstract

Intrinsically disordered proteins (IDPs) inhabit a conformational landscape that is too complex to be described by classical structural biology, posing an entirely new set of questions concerning the molecular understanding of functional biology. The characterization of the conformational properties of IDPs, and the elucidation of the role they play in molecular function, is therefore one of the major challenges remaining for modern structural biology. NMR is the technique of choice for studying this class of proteins, providing information about structure, flexibility, and interactions at atomic resolution even in completely disordered states. In particular, residual dipolar couplings (RDCs) have been shown to be uniquely sensitive and powerful tools for characterizing local and long-range structural behavior in disordered proteins. In this review we describe recent applications of RDCs to quantitatively describe the level of local structure and transient long-range order in IDPs involved in viral replication, neurodegenerative disease, and cancer.

PMID:: 19748338; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances

Publication Types

Review

MeSH Terms

Substances

Tumor Suppressor Protein p53

LinkOut - more resources

Full Text Sources

Other Literature Sources

COS Scholar Universe

Supplemental Content

Save items

Related citations in PubMed

Review Structural disorder within sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition. [Protein Pept Lett. 2010]
Review Structural disorder within sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition.
Jensen MR, Bernadó P, Houben K, Blanchard L, Marion D, Ruigrok RW, Blackledge M. Protein Pept Lett. 2010 Aug; 17(8):952-60.
NMR characterization of long-range order in intrinsically disordered proteins. [J Am Chem Soc. 2010]
NMR characterization of long-range order in intrinsically disordered proteins.
Salmon L, Nodet G, Ozenne V, Yin G, Jensen MR, Zweckstetter M, Blackledge M. J Am Chem Soc. 2010 Jun 23; 132(24):8407-18.
Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts. [J Am Chem Soc. 2010]
Defining conformational ensembles of intrinsically disordered and partially folded proteins directly from chemical shifts.
Jensen MR, Salmon L, Nodet G, Blackledge M. J Am Chem Soc. 2010 Feb 3; 132(4):1270-2.
Conformational distributions of unfolded polypeptides from novel NMR techniques. [J Chem Phys. 2008]
Conformational distributions of unfolded polypeptides from novel NMR techniques.
Meier S, Blackledge M, Grzesiek S. J Chem Phys. 2008 Feb 7; 128(5):052204.
Review Residual dipolar couplings in NMR structure analysis. [Annu Rev Biophys Biomol Struct...]
Review Residual dipolar couplings in NMR structure analysis.
Lipsitz RS, Tjandra N. Annu Rev Biophys Biomol Struct. 2004; 33:387-413.

See reviews... See all...

Cited by 10 PubMed Central articles

Relative solvent accessible surface area predicts protein conformational changes upon binding. [Structure. 2011]
Relative solvent accessible surface area predicts protein conformational changes upon binding.
Marsh JA, Teichmann SA. Structure. 2011 Jun 8; 19(6):859-67.
Intrinsic disorder in measles virus nucleocapsids. [Proc Natl Acad Sci U S A. 2011]
Intrinsic disorder in measles virus nucleocapsids.
Jensen MR, Communie G, Ribeiro EA Jr, Martinez N, Desfosses A, Salmon L, Mollica L, Gabel F, Jamin M, Longhi S, et al. Proc Natl Acad Sci U S A. 2011 Jun 14; 108(24):9839-44. Epub 2011 May 25.
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices. [Protein Sci. 2011]
The N(0)-binding region of the vesicular stomatitis virus phosphoprotein is globally disordered but contains transient α-helices.
Leyrat C, Jensen MR, Ribeiro EA Jr, Gérard FC, Ruigrok RW, Blackledge M, Jamin M. Protein Sci. 2011 Mar; 20(3):542-56. Epub 2011 Feb 16.

See all...

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.

Recent activity

Clear Turn Off Turn On

Quantitative determination of the conformational properties of partially folded ...
Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings.
Structure. 2009 Sep 9 ;17(9):1169-85.

PubMed
Polyglutamine dances the conformational cha-cha-cha.
Polyglutamine dances the conformational cha-cha-cha.
Structure. 2009 Sep 9 ;17(9):1151-3.

PubMed
Long-term effect of early treatment with interferon beta-1b after a first clinic...
Long-term effect of early treatment with interferon beta-1b after a first clinical event suggestive of multiple sclerosis: 5-year active treatment extension of the phase 3 BENEFIT trial.
Lancet Neurol. 2009 Nov ;8(11):987-97. Epub 2009 Sep 10 .

PubMed
Similarities in features of autism and asthma and a possible link to acetaminoph...
Similarities in features of autism and asthma and a possible link to acetaminophen use.
Med Hypotheses. 2010 Jan ;74(1):7-11. Epub 2009 Sep 11 .

PubMed
Typical pollutants in bottom ashes from a typical medical waste incinerator.
Typical pollutants in bottom ashes from a typical medical waste incinerator.
J Hazard Mater. 2010 Jan 15 ;173(1-3):181-5. Epub 2009 Aug 22 .

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Result Filters

Display Settings:

Send to: