NMR has emerged as an important tool for studies of protein folding because of the unique structural insights it can provide into many aspects of the folding process. Applications include measurements of kinetic folding events and structural characterization of folding intermediates, partly folded states, and unfolded states. Kinetic information on a time scale of milliseconds or longer can be obtained by real-time NMR experiments and by quench-flow hydrogen-exchange pulse labeling. Although NMR cannot provide direct information on the very rapid processes occurring during the earliest stages of protein folding, studies of isolated peptide fragments provide insights into likely protein folding initiation events. Multidimensional NMR techniques are providing new information on the structure and dynamics of protein folding intermediates and both partly folded and unfolded states.
[NMR images] Protein folding technology
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Protein folding technology
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[NMR paper] NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformation
NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
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J Biol Chem. 2004 Aug 13;279(33):34963-70
Authors: Santiveri CM, Pérez-Cañadillas JM, Vadivelu MK, Allen MD, Rutherford TJ, Watkins NA, Bycroft M
The structure of alpha-hemoglobin stabilizing protein (AHSP), a molecular chaperone for free alpha-hemoglobin, has been determined using NMR spectroscopy....
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11-24-2010 09:51 PM
[NMR paper] Insights into the interactions between a drug and a membrane protein target by fluori
Insights into the interactions between a drug and a membrane protein target by fluorine cross-polarization magic angle spinning NMR.
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Magn Reson Chem. 2004 Feb;42(2):204-11
Authors: Boland MP, Middleton DA
The fluorinated anti-psychotic drug trifluoperazine (TFP) has been shown to be a K(+)-competitive inhibitor of gastric H(+)/K(+)-ATPase, a membrane-embedded therapeutic target for peptic ulcer...
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[NMR paper] Insights into conformation and dynamics of protein GB1 during folding and unfolding b
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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] New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
New structural insights into carbohydrate-protein interactions from NMR spectroscopy.
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Curr Opin Struct Biol. 2003 Oct;13(5):646-53
Authors: Kogelberg H, Solís D, Jiménez-Barbero J
Recently developed NMR methods have been applied to discover carbohydrate ligands for proteins and to identify their binding epitopes. The structural details of carbohydrate-protein complexes have also been examined by NMR, providing site-specific information on the...
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11-24-2010 09:16 PM
[NMR paper] NMR investigations of protein-carbohydrate interactions: insights into the topology o
NMR investigations of protein-carbohydrate interactions: insights into the topology of the bound conformation of a lactose isomer and beta-galactosyl xyloses to mistletoe lectin and galectin-1.
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Biochim Biophys Acta. 2001 Dec 19;1568(3):225-36
Authors: Alonso-Plaza JM, Canales MA, Jiménez M, Roldán JL, García-Herrero A, Iturrino L, Asensio JL,...
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[NMR paper] Insights into tyrosine phosphorylation control of protein-protein association from th
Insights into tyrosine phosphorylation control of protein-protein association from the NMR structure of a band 3 peptide inhibitor bound to glyceraldehyde-3-phosphate dehydrogenase.
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Biochemistry. 1998 Jan 20;37(3):867-77
Authors: Eisenmesser EZ, Post CB
A protein-protein association regulated by phosphorylation of tyrosine is examined by NMR...
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[NMR paper] Contacting the protein folding funnel with NMR.
Contacting the protein folding funnel with NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Contacting the protein folding funnel with NMR.
Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7129-31
Authors: Onuchic JN
Insights into protein folding from NMR.
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