Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
Non-Native Interactions in the FF Domain Folding Pathway From an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study.
J Am Chem Soc. 2011 Jun 6;
Authors: Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE
Several all-helical single-domain proteins have been shown to fold rapidly (us timescale) to a compact...
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06-07-2011 11:05 AM
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation.
Protein Sci. 2011 Feb;20(2):229-46
Authors: Clore GM
Sparsely populated states of macromolecules, characterized by short lifetimes and high free-energies relative to the predominant ground state, often play a key role in many biological, chemical, and biophysical processes. In this review, we briefly summarize various new developments in NMR...
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06-04-2011 11:26 AM
[NMR paper] NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
Related Articles NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
J Am Chem Soc. 2005 Sep 28;127(38):13207-12
Authors: Zeeb M, Balbach J
The cold shock protein CspB adopts its native and functional tertiary structure on the millisecond time scale. We employed transverse relaxation NMR methods, which allow a quantitative measurement of the cooperativity of this...
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12-01-2010 06:56 PM
[NMR paper] An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mu
An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
Related Articles An 15N NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b562.
J Am Chem Soc. 2005 Apr 13;127(14):5066-72
Authors: Choy WY, Zhou Z, Bai Y, Kay LE
15N relaxation dispersion NMR spectroscopy has been used to study exchange dynamics in a pair of mutants of Rd-apocyt b562, a redesigned four-helix-bundle protein. An analysis of the relaxation data over a range of...
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11-25-2010 08:21 PM
[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Biochemistry. 2004 Nov 2;43(43):13775-86
Authors: Bann JG, Frieden C
The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...
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11-24-2010 10:03 PM
[NMR paper] Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
Related Articles Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.
Nature. 2004 Jul 29;430(6999):586-90
Authors: Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE
Many biochemical processes proceed through the formation of functionally significant intermediates. Although the identification and characterization of such species can provide vital clues about the mechanisms of the...
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11-24-2010 09:51 PM
[NMR paper] A protein folding intermediate of ribonuclease T1 characterized at high resolution by
A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy.
Related Articles A protein folding intermediate of ribonuclease T1 characterized at high resolution by 1D and 2D real-time NMR spectroscopy.
J Mol Biol. 1999 Jan 15;285(2):829-42
Authors: Balbach J, Steegborn C, Schindler T, Schmid FX
The rate-limiting step during the refolding of S54G/P55N ribonuclease T1 is determined by the slow trans-->cis prolyl isomerisation of Pro39. We investigated the refolding of this variant by...
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11-18-2010 07:05 PM
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Sec
A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution - Securities Industry News (blog) (subscription)
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A Transient and Low-Populated Protein-Folding Intermediate at Atomic Resolution
Securities Industry News (blog) (subscription)
In this work, we used chemical shifts and bond-vector orientation constraints obtained from nuclear magnetic resonance relaxation dispersion spectroscopy, ...
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Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
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