Related ArticlesHydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Sci. 1997 Jun;6(6):1316-24
Authors: Chung EW, Nettleton EJ, Morgan CJ, Gross M, Miranker A, Radford SE, Dobson CM, Robinson CV
The extent of deuterium labeling of hen lysozyme, its three-disulfide derivative, and the homologous alpha-lactalbumins, has been measured by both mass spectrometry and NMR. Different conformational states of the proteins were produced by varying the solution conditions. Alternate protein conformers were found to contain different numbers of 2H atoms. Furthermore, measurement in the gas phase of the mass spectrometer or directly in solution by NMR gave consistent results. The unique ability of mass spectrometry to distinguish distributions of 2H atoms in protein molecules is exemplified using samples prepared to contain different populations of 2H-labeled protein. A comparison of the peak widths of bovine alpha-lactalbumin in alternate solution conformations but containing the same average number of 2H atoms showed dramatic differences due to different 2H distributions in the two protein conformers. Measurement of 2H distributions by ESI-MS enabled characterization of conformational averaging and structural heterogeneity. In addition, a time course for hydrogen exchange was examined and the variation in distributions of 2H atom compared with simulations for different hydrogen exchange models. The results clearly show that exchange from the native state of bovine alpha-lactalbumin at 15 degrees C is dominated by local unfolding events.
[NMR paper] Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Related Articles Ribonuclease Sa conformational stability studied by NMR-monitored hydrogen exchange.
Biochemistry. 2005 May 31;44(21):7644-55
Authors: Laurents DV, Scholtz JM, Rico M, Pace CN, Bruix M
The conformational stability of ribonuclease Sa (RNase Sa) has been measured at the per-residue level by NMR-monitored hydrogen exchange at pH* 5.5 and 30 degrees C. In these conditions, the exchange mechanism was found to be EXII. The conformational stability...
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11-25-2010 08:21 PM
[NMR paper] Hydrodynamic radii of native and denatured proteins measured by pulse field gradient
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
Related Articles Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques.
Biochemistry. 1999 Dec 14;38(50):16424-31
Authors: Wilkins DK, Grimshaw SB, Receveur V, Dobson CM, Jones JA, Smith LJ
Pulse field gradient NMR methods have been used to determine the effective hydrodynamic radii of a range of native and nonnative protein conformations. From these experimental data, empirical relationships...
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11-18-2010 08:31 PM
[NMR paper] Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier
Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy.
Related Articles Pressure-denatured state of Escherichia coli ribonuclease HI as monitored by Fourier transform infrared and NMR spectroscopy.
Biochemistry. 1998 Dec 22;37(51):18001-9
Authors: Yamasaki K, Taniguchi Y, Takeda N, Nakano K, Yamasaki T, Kanaya S, Oobatake M
Pressure denaturation of Escherichia coli ribonuclease HI (RNase HI) was studied by Fourier transform infrared (FTIR) and two-dimensional NMR...
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11-17-2010 11:15 PM
[NMR paper] Hydrogen exchange properties of proteins in native and denatured states monitored by
Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
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 Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMR.
Protein Sci. 1997 Jun;6(6):1316-24
Authors: Chung EW,...
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08-22-2010 03:31 PM
[NMR paper] Structural analysis of non-native states of proteins by NMR methods.
Structural analysis of non-native states of proteins by NMR methods.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural analysis of non-native states of proteins by NMR methods.
Curr Opin Struct Biol. 1996 Feb;6(1):24-30
Authors: Shortle DR
Established NMR methods are increasingly being applied to the non-native states of proteins. For small denatured proteins, full assignment of proton, 15N and 13C resonances is often straightforward. Sensitive methods exist...
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08-22-2010 02:27 PM
[MWClarkson blog] How native-like is a cold-denatured structure?
How native-like is a cold-denatured structure?
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngA protein has several different levels of structure. The primary structure is the arrangements of atoms and bonds, and it is formed in the ribosome by the assembly of amino acids as directed by an RNA template. The secondary structure is the local topology, the helices and strands, and this forms mostly because of the release of energy through the formation of hydrogen bonds. The tertiary structure is the actual fold of the protein, the way helices, strands, and loops are...
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08-22-2010 01:58 AM
[NMR paper] Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.
Related Articles Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR.
Biochemistry. 1990 Nov 20;29(46):10433-7
Authors: Jeng MF, Englander SW, Elöve GA, Wand AJ, Roder H
Hydrogen exchange and two-dimensional nuclear magnetic resonance (2D NMR) techniques were used to characterize the structure of oxidized horse cytochrome c at acid pH and high ionic strength. Under these conditions, cytochrome c is known to assume a...
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08-21-2010 11:04 PM
[NMR paper] Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e
Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
FEBS Lett. 1999 Feb 26;445(2-3):361-5
Authors: Jonasson P, Kjellsson A, Sethson I, Jonsson BH
Hydrogen/deuterium (H/D) exchange measurements in low and moderate...