NMR paper Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with seq

		BioNMR > Educational resources > Journal club
[NMR paper] Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with seq

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, 03:01 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with seq

Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with sequence-specific assignments.

Related Articles Localisation of methionine residues in bacteriorhodopsin by carbonyl 13C-NMR with sequence-specific assignments.

FEBS Lett. 1993 Jul 19;327(1):7-12

Authors: Seigneuret M, Kainosho M

High-resolution 13C-NMR experiments have been performed on bacteriorhodopsin biosynthetically labeled with carbonyl-13C amino acids and solubilized in the detergent dodecylmaltoside. 13C-NMR spectra showing good resolution were obtained in the case of labeled amino acids moderately represented in the BR sequence. For BR labeled with [13C]carbonyl methionine, several sequence-specific assignment could be performed by co-labeling with 15N amino acids or proteolysis. These assignments were used to obtain structural data on BR. Water-exposure of methionine side chains in the protein was assessed by studying, using NMR, their oxidation by hydrogen peroxide. Local secondary structure at the level of methionine residues was monitored through the effect of 1H-2H exchange on NMR spectra. It was concluded that Met32, Met68 and Met163 are peripheral while all 6 other methionine residues are deeply embedded within hydrophobic alpha-helices. These results confirm the current model of the BR folding and secondary structure.

PMID: 8335098 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Fast methionine-based solution structure determination of calcium-calmodulin complexes Fast methionine-based solution structure determination of calcium-calmodulin complexes Abstract Here we present a novel NMR method for the structure determination of calcium-calmodulin (Ca2+-CaM)-peptide complexes from a limited set of experimental restraints. A comparison of solved CaM-peptide structures reveals invariability in CaMâ??s backbone conformation and a structural plasticity in CaMâ??s domain orientation enabled by a flexible linker. Knowing this, the collection and analysis of an extensive set of NOESY spectra is redundant. Although RDCs can define CaM domain orientation in...	nmrlearner	Journal club	0	03-03-2011 02:06 AM
[NMR paper] Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determina Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determinants for conformation and dynamics as revealed by site-directed solid-state 13C NMR. Related Articles Glutamic acid residues of bacteriorhodopsin at the extracellular surface as determinants for conformation and dynamics as revealed by site-directed solid-state 13C NMR. Biophys J. 2004 Mar;86(3):1673-81 Authors: Saitô H, Yamaguchi S, Ogawa K, Tuzi S, Márquez M, Sanz C, Padrós E We recorded (13)C NMR spectra of Ala- and Val-labeled bacteriorhodopsin (bR) and a...	nmrlearner	Journal club	0	11-24-2010 09:25 PM
[NMR paper] [13C]Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride. Related Articles Methionine NMR and metal-binding studies of recombinant human transferrin N-lobe and five methionine mutants: conformational changes and increased sensitivity to chloride. Biochem J. 1999 Dec 15;344 Pt 3:881-7 Authors: He QY, Mason AB, Tam BM, MacGillivray RT, Woodworth RC The N-lobe of human serum transferrin (hTF/2N) and single point mutants in which each...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
Conformational dependence of 13C shielding and coupling constants for methionine Abstract Methionine residues fulfill a broad range of roles in protein function related to conformational plasticity, ligand binding, and sensing/mediating the effects of oxidative stress. A high degree of internal mobility, intrinsic detection sensitivity of the methyl group, and low copy number have made methionine labeling a popular approach for NMR investigation of selectively labeled protein macromolecules. However, selective labeling approaches are subject to more limited information content. In order to optimize the information available from such studies, we have performed DFT...	nmrlearner	Journal club	0	08-25-2010 03:51 PM
[NMR paper] Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterizati Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions. Biochemistry. 1996 Oct 22;35(42):13627-35 Authors: Barker PD, Freund SM Previous work has shown that, in variants of cytochrome b562 containing the H102M mutation, methionine residues provide both...	nmrlearner	Journal club	0	08-22-2010 02:20 PM
[NMR paper] NMR studies of the methionine methyl groups in calmodulin. NMR studies of the methionine methyl groups in calmodulin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR studies of the methionine methyl groups in calmodulin. FEBS Lett. 1995 Jun 12;366(2-3):104-8 Authors: Siivari K, Zhang M, Palmer AG, Vogel HJ Calmodulin (CaM) is a ubiquitous Ca(2+)-binding protein that can regulate a wide variety of cellular events. The protein contains 9 Met out of a total of 148 amino acid residues. The binding of Ca2+ to CaM induces...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] High-resolution 13C NMR study of the topography and dynamics of methionine residues i High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin. Related Articles High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin. Biochemistry. 1991 Apr 23;30(16):3885-92 Authors: Seigneuret M, Neumann JM, Levy D, Rigaud JL The proton transport membrane protein bacteriorhodopsin has been biosynthetically labeled with methionine and studied by high-resolution 13C NMR after solubilization in the detergent...	nmrlearner	Journal club	0	08-21-2010 11:16 PM
[NMR paper] Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Surface exposure of the methionine side chains of calmodulin in solution. A nitroxide spin label and two-dimensional NMR study. J Biol Chem. 1999 Mar 26;274(13):8411-20 Authors: Yuan T, Ouyang H, Vogel HJ Binding of calcium to calmodulin (CaM) causes a conformational...	nmrlearner	Journal club	0	08-21-2010 04:03 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