NMR paper Probing protein structure by solvent perturbation of NMR spectra. Photochemically ind

		BioNMR > Educational resources > Journal club
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. Photochemically ind

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-22-2010, 03:41 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Probing protein structure by solvent perturbation of NMR spectra. Photochemically ind

Probing protein structure by solvent perturbation of NMR spectra. Photochemically induced dynamic nuclear polarization and paramagnetic perturbation techniques applied to the study of the molten globule state of alpha-lactalbumin.

Related Articles Probing protein structure by solvent perturbation of NMR spectra. Photochemically induced dynamic nuclear polarization and paramagnetic perturbation techniques applied to the study of the molten globule state of alpha-lactalbumin.

Eur J Biochem. 1995 Jan 15;227(1-2):87-96

Authors: Improta S, Molinari H, Pastore A, Consonni R, Zetta L

We have characterized the high-temperature molten globule state of bovine alpha-lactalbumin by a combined use of photochemically induced dynamic nuclear polarization and nitroxide surface perturbation. Both techniques are extremely well suited to follow the progressive increase of exposed surfaces in the native state and the appearance of partially or completely unfolded species. Our results suggest that the molten globule state obtained at high temperature and pH 7, and the state obtained at pH 2 are not only thermodynamically but also structurally very similar.

PMID: 7851446 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra. Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra. Singular spectrum analysis for an automated solvent artifact removal and baseline correction of 1D NMR spectra. J Magn Reson. 2011 Mar 6; Authors: De Sanctis S, Malloni WM, Kremer W, Tomé AM, Lang EW, Neidig KP, Kalbitzer HR NMR spectroscopy in biology and medicine is generally performed in aqueous solutions, thus in (1)H NMR spectroscopy, the dominant signal often stems from the partly suppressed solvent and can be many orders of...	nmrlearner	Journal club	0	04-05-2011 10:22 PM
[NMR paper] Probing membrane protein orientation and structure using fast magic-angle-spinning so Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR. Related Articles Probing membrane protein orientation and structure using fast magic-angle-spinning solid-state NMR. J Biomol NMR. 2004 Nov;30(3):253-65 Authors: Andronesi OC, Pfeifer JR, Al-Momani L, Ozdirekcan S, Rijkers DT, Angerstein B, Luca S, Koert U, Killian JA, Baldus M One and two-dimensional solid-state NMR experiments are discussed that permit probing local structure and overall molecular conformation of membrane-embedded polypeptides...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. Related Articles Probing solvent accessibility of transthyretin amyloid by solution NMR spectroscopy. J Biol Chem. 2004 Feb 13;279(7):5699-707 Authors: Olofsson A, Ippel JH, Wijmenga SS, Lundgren E, Ohman A The human plasma protein transthyretin (TTR) may form fibrillar protein deposits that are associated with both inherited and idiopathic amyloidosis. The present study utilizes solution nuclear magnetic resonance spectroscopy, in combination with...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy. Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy. Related Articles Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy. Proc Natl Acad Sci U S A. 2002 Jun 25;99(13):8648-53 Authors: Ippel JH, Olofsson A, Schleucher J, Lundgren E, Wijmenga SS Amyloid is the result of an anomalous protein and peptide aggregation, leading to the formation of insoluble fibril deposits. At present, 18 human diseases have been associated with amyloid deposits-e.g., Alzheimer's disease and Prion-transmissible...	nmrlearner	Journal club	0	11-24-2010 08:49 PM
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra: the surface accessi Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor. Biophys J. 1997 Jul;73(1):382-96 Authors: Molinari H,...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra: the surface accessi Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor. Biophys J. 1997 Jul;73(1):382-96 Authors: Molinari H,...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. A comparison with p Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Probing protein structure by solvent perturbation of NMR spectra. A comparison with photochemically induced dynamic nuclear polarization techniques applied to native alpha-lactalbumin. Eur J Biochem. 1995 Jan 15;227(1-2):78-86...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] Probing protein structure by solvent perturbation of NMR spectra. II. Determination o Probing protein structure by solvent perturbation of NMR spectra. II. Determination of surface and buried residues in homologous proteins. Related Articles Probing protein structure by solvent perturbation of NMR spectra. II. Determination of surface and buried residues in homologous proteins. Biopolymers. 1993 May;33(5):839-46 Authors: Esposito G, Lesk AM, Molinari H, Motta A, Niccolai N, Pastore A The experimental assignment of most residues in a protein to the surface or interior is in principle possible without prior solution of a complete...	nmrlearner	Journal club	0	08-21-2010 11:53 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off