Related ArticlesDetection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR.
Biochemistry. 1992 May 26;31(20):4749-56
Authors: Lu J, Dahlquist FW
Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme. In the unfolded state, there is little differential protection of the various amides from hydrogen exchange. In the native folded structure, 84 amides of the 164 residues are sufficiently spectrally resolved and protected from solvent exchange to serve as probes of the folding pathway. These probes are located in both the N-terminal and C-terminal domains of the native folded structure of the protein. The studies described here show that at least one intermediate is formed early during refolding at low denaturant concentrations. This intermediate (or intermediates) forms very rapidly (within the 10-ms temporal resolution of our mixing device) under the conditions used and is completed at least 10 times faster than the overall folding event. The intermediate(s) protect(s) from exchange a subset of amides in the N-terminal and C-terminal regions of the protein. In the final folded states these protected regions correspond to two alpha-helices and a beta-sheet region. These amides are protected from exchange by factors between 20 and 200 as compared to the fully unfolded protein. Protection of this magnitude is consistent with the formation of somewhat exposed secondary structure in these regions and could represent a "molten globule"-like or a "framework"-like structure for the intermediate(s) in which specific parts of the sequence form isolated secondary structures that are not stabilized by extensive tertiary interactions.
[NMR paper] NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
Related Articles NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor.
Structure. 2005 Aug;13(8):1193-202
Authors: Arolas JL, D'Silva L, Popowicz GM, Aviles FX, Holak TA, Ventura S
The III-A intermediate constitutes the major rate-determining step in the oxidative folding of leech carboxypeptidase inhibitor...
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[NMR paper] NMR elucidation of early folding hierarchy in HIV-1 protease.
NMR elucidation of early folding hierarchy in HIV-1 protease.
Related Articles NMR elucidation of early folding hierarchy in HIV-1 protease.
J Biol Chem. 2003 May 30;278(22):19980-5
Authors: Bhavesh NS, Sinha R, Mohan PM, Hosur RV
Folding studies on proteases by the conventional hydrogen exchange experiments are severely hampered because of interference from the autolytic reaction in the interpretation of the exchange data. We report here NMR identification of the hierarchy of early conformational transitions (folding propensities) in HIV-1...
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[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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Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Related Articles Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Biochemistry. 2010 Sep 15;
Authors: Chang YC, Franch WR, Oas TG
Protein folding intermediates are often imperative to overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder the biochemical and biophysical characterization. Previous studies have demonstrated that Bacillus...
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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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[NMR paper] Demonstration by NMR of folding domains in lysozyme.
Demonstration by NMR of folding domains in lysozyme.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles Demonstration by NMR of folding domains in lysozyme.
Nature. 1991 Feb 14;349(6310):633-6
Authors: Miranker A, Radford SE, Karplus M, Dobson CM
Although there has been much speculation on the pathways of protein folding, only recently have experimental data on the topic been available. The study of proteins under conditions where species intermediate between the fully folded and...
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[NMR paper] Detection and characterization of a folding intermediate in barnase by NMR.
Detection and characterization of a folding intermediate in barnase by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles Detection and characterization of a folding intermediate in barnase by NMR.
Nature. 1990 Aug 2;346(6283):488-90
Authors: Bycroft M, Matouschek A, Kellis JT, Serrano L, Fersht AR
Protein engineering is being developed for mapping the energetics and pathway of protein folding. From kinetic studies on wild-type and mutant proteins, the sequence and energetics of...
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[NMR paper] Real-time NMR studies on a transient folding intermediate of barstar.
Real-time NMR studies on a transient folding intermediate of barstar.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Real-time NMR studies on a transient folding intermediate of barstar.
Protein Sci. 1999 Jun;8(6):1286-91
Authors: Killick TR, Freund SM, Fersht AR
The refolding of barstar, the intracellular...
Detection and characterization of an early folding intermediate of T4 lysozyme using
Linear Mode
