Related ArticlesMechanical unfolding of a titin Ig domain: structure of unfolding intermediate revealed by combining AFM, molecular dynamics simulations, NMR and protein engineering.
J Mol Biol. 2002 Sep 27;322(4):841-9
Authors: Fowler SB, Best RB, Toca Herrera JL, Rutherford TJ, Steward A, Paci E, Karplus M, Clarke J
The mechanical unfolding of an immunoglobulin domain from the human muscle protein titin (TI I27) has been shown to proceed via a metastable intermediate in which the A-strand is detached. The structure and properties of this intermediate are characterised in this study. A conservative destabilising mutation in the A-strand has no effect on the unfolding force, nor the dependence of the unfolding force on the pulling speed, indicating that the unfolding forces measured in an AFM experiment are those required for the unfolding of the intermediate and not the native state. A mutant of TI I27 with the A-strand deleted (TI I27-A) is studied by NMR and standard biophysical techniques, combined with protein engineering. Molecular dynamics simulations show TI I27-A to be a good model for the intermediate. It has a structure very similar to the native state, and is surprisingly stable. Comparison with a Phi-value analysis of the unfolding pathway clearly shows that the protein unfolds by a different pathway under an applied force than on addition of denaturant.
Domain Swapping Proceedsvia Complete Unfolding: A 19F- and 1H-NMR Studyof the Cyanovirin-N Protein
Domain Swapping Proceedsvia Complete Unfolding: A 19F- and 1H-NMR Studyof the Cyanovirin-N Protein
Lin Liu, In-Ja L. Byeon, Ivet Bahar and Angela M. Gronenborn
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja210118w/aop/images/medium/ja-2011-10118w_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja210118w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/vh5BfRyKD-8
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Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Long-Lived States to Monitor Protein Unfolding by Proton NMR.
Chemphyschem. 2011 Aug 31;
Authors: Bornet A, Ahuja P, Sarkar R, Fernandes L, Hadji S, Lee SY, Haririnia A, Fushman D, Bodenhausen G, Vasos PR
Abstract
The relaxation of long-lived states (LLS) corresponds to the slow return to statistical thermal equilibrium between symmetric and antisymmetric proton spin states. This process is remarkably sensitive to the presence of external spins and can be used to obtain...
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[NMR paper] The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR da
The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR data.
Related Articles The equilibrium unfolding of MerP characterized by multivariate analysis of 2D NMR data.
J Magn Reson. 2005 Jan;172(1):24-30
Authors: Berglund A, Brorsson AC, Jonsson BH, Sethson I
A general problem when analysing NMR spectra that reflect variations in the environment of target molecules is that different resonances are affected to various extents. Often a few resonances that display the largest frequency changes are selected as probes to...
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[NMR paper] Insights into conformation and dynamics of protein GB1 during folding and unfolding b
Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR.
Related Articles Insights into conformation and dynamics of protein GB1 during folding and unfolding by NMR.
J Mol Biol. 2004 Jan 30;335(5):1299-307
Authors: Ding K, Louis JM, Gronenborn AM
Understanding protein stability requires characterization of structural determinants of the folded and unfolded states. Many proteins are capable of populating partially folded states under specific solution conditions. Occasionally, coexistence of the folded and an...
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[NMR paper] A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydro
A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles A 19F-NMR study of the equilibrium unfolding of membrane-associated D-lactate dehydrogenase of Escherichia coli.
Biochemistry. 1996 Dec 24;35(51):16502-9
Authors: Sun ZY, Pratt EA, Simplaceanu V, Ho C
Partially folded protein intermediates have been observed by 19F-NMR spectroscopy during the equilibrium unfolding of the...
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[NMR paper] NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
Related Articles NMR study of the cold, heat, and pressure unfolding of ribonuclease A.
Biochemistry. 1995 Jul 11;34(27):8631-41
Authors: Zhang J, Peng X, Jonas A, Jonas J
The reversible cold, heat, and pressure unfolding of RNase A and RNase A--inhibitor complex were studied by 1D and 2D 1H NMR spectroscopy. The reversible pressure denaturation experiments in the pressure range from 1 bar to 5 kbar were carried out at pH 2.0 and 10 degrees C. The cold denaturation was...
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[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3880-5
Authors: Spooner PJ, Watts A
31P NMR measurements were conducted to determine the structural and chemical environment of beef heart cardiolipin when bound to cytochrome c. 31P NMR line shapes infer that the majority of lipid remains...
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[NMR paper] Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. E
Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Related Articles Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements.
Biochemistry. 1991 Apr 23;30(16):3871-9
Authors: Spooner PJ, Watts A
Deuterium NMR has been used to investigate the structure and dynamic state of cytochrome c complexed with bilayers of cardiolipin. Reductive methylation was employed to prepare lysyl cytochrome c, and deuterium...