NMR paper NMR studies of the methionine methyl groups in calmodulin.

		BioNMR > Educational resources > Journal club
[NMR paper] NMR studies of the methionine methyl groups in calmodulin.

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-22-2010, 03:41 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,178

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

NMR studies of the methionine methyl groups in calmodulin.

NMR studies of the methionine methyl groups in calmodulin.

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 conformational changes and exposes two Met-rich hydrophobic surfaces which provide the main protein-protein contact areas when CaM interacts with its target enzymes. Two-dimensional (1H,13C)-heteronuclear multiple quantum coherence (HMQC) NMR spectroscopy was used to study selectively 13C-isotope labelled Met methyl groups in apo-CaM, Ca(2+)-CaM and a complex of CaM with the CaM-binding domain of skeletal muscle Myosin Light Chain Kinase (MLCK). The resonance assignment of the Met methyl groups in these three functionally different states were obtained by site-directed mutagenesis (Met-->Leu). Chemical shift changes indicate that the methyl groups of the Met residues are in different environments in apo-, calcium-, and MLCK-bound-CaM. The T1 relaxation rates of the individual Met methyl carbons in the three forms of CaM indicate that those in Ca(2+)-CaM have the highest mobility. Our results also suggest that the methyl groups of the unbranched Met sidechains in general are more flexible than those of aliphatic amino acid residues such as Leu and Ile.

PMID: 7789524 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins. An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins. An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins. Chem Commun (Camb). 2011 Jul 26; Authors: Ayala I, Hamelin O, Amero C, Pessey O, Plevin MJ, Gans P, Boisbouvier J An efficient synthetic route is proposed to produce 2-hydroxy-2-ethyl-3-oxobutanoate for the specific labelling of Ile methyl-?(2) groups in proteins. The (2)H,...	nmrlearner	Journal club	0	07-28-2011 10:51 AM
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
A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins A simple biosynthetic method for stereospecific resonance assignment of prochiral methyl groups in proteins Abstract A new method for stereospecific assignment of prochiral methyl groups in proteins is presented in which protein samples are produced using U-glucose and subsaturating amounts of 2-methyl-acetolactate. The resulting non-uniform labeling pattern allows proR and proS methyl groups to be easily distinguished by their different phases in a constant-time two-dimensional 1H-13C correlation spectra. Protein samples are conveniently prepared using the same media composition as the...	nmrlearner	Journal club	0	02-06-2011 07:42 PM
Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins Selective 1H-13C NMR spectroscopy of methyl groups in residually protonated samples of large proteins Abstract Methyl 13CHD2 isotopomers of all methyl-containing amino-acids can be observed in residually protonated samples of large proteins obtained from -glucose/D2O-based bacterial media, with sensitivity sufficient for a number of NMR applications. Selective detection of some subsets of methyl groups (AlaÎ², ThrÎ³2) is possible using simple â??out-and-backâ?? NMR methodology. Such selective methyl-detected â??out-and-backâ?? NMR experiments allow complete assignments of threonine Î³2...	nmrlearner	Journal club	0	01-09-2011 12:46 PM
Methyl groups as probes of supra-molecular structure, dynamics and function Methyl groups as probes of supra-molecular structure, dynamics and function Abstract The development of new protein labeling strategies, along with optimized experiments that exploit the label, have significantly impacted on the types of biochemical problems that can now be addressed by solution NMR spectroscopy. Here we describe how methyl labeling of key residues in a highly deuterated protein background has facilitated studies of the structure, dynamics and interactions of supra-molecular particles. The methyl-labeling approach is briefly reviewed, followed by a summary of...	nmrlearner	Journal club	0	01-09-2011 12:46 PM
[NMR paper] Methyl groups as probes for proteins and complexes in in-cell NMR experiments. Methyl groups as probes for proteins and complexes in in-cell NMR experiments. Related Articles Methyl groups as probes for proteins and complexes in in-cell NMR experiments. J Am Chem Soc. 2004 Jun 9;126(22):7119-25 Authors: Serber Z, Straub W, Corsini L, Nomura AM, Shimba N, Craik CS, Ortiz de Montellano P, Dötsch V Studying protein components of large intracellular complexes by in-cell NMR has so far been impossible because the backbone resonances are unobservable due to their slow tumbling rates. We describe a methodology that overcomes...	nmrlearner	Journal club	0	11-24-2010 09:51 PM
[NMR paper] Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in Cross-correlated relaxation enhanced 1H13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. Related Articles Cross-correlated relaxation enhanced 1H13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc. 2003 Aug 27;125(34):10420-8 Authors: Tugarinov V, Hwang PM, Ollerenshaw JE, Kay LE A comparison of HSQC and HMQC pulse schemes for recording (1)H(13)C correlation maps of protonated methyl groups in highly deuterated proteins is presented....	nmrlearner	Journal club	0	11-24-2010 09:16 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