NMR paper Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colic

		BioNMR > Educational resources > Journal club
[NMR paper] Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colic

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

11-19-2010, 08:32 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,733

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

Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colic

Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.

Related Articles Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain.

Biochemistry. 2001 Jun 26;40(25):7662-74

Authors: Huster D, Xiao L, Hong M

Solid-state NMR spectroscopy was employed to study the molecular dynamics of the colicin Ia channel domain in the soluble and membrane-bound states. In the soluble state, the protein executes small-amplitude librations (with root-mean-square angular fluctuations of 0-10 degrees ) in the backbone and larger-amplitude motions (16-17 degrees ) in the side chains. Upon membrane binding, the motional amplitudes increase significantly for both the backbone (12-16 degrees ) and side chains (23-29 degrees ), as manifested by the reduction in the C-H and H-H dipolar couplings and (15)N chemical shift anisotropy. These motions occur not only on the pico- to nanosecond time scales, but also on the microsecond time scale, as revealed by the (1)H rotating-frame spin-lattice relaxation times. Average motional correlation times of 0.8 and 1.2 micros were extracted for the soluble and membrane-bound states, respectively. In comparison, both forms of the colicin Ia channel domain are completely immobile on the millisecond scale. These results indicate that the colicin Ia channel domain has enhanced conformational mobility in the lipid bilayer compared to the soluble state. This membrane-induced mobility increase is consistent with the loss of tertiary structure of the protein in the membrane, which was previously suggested by the extended helical array model [Zakharov et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4282-4287]. An extended structure would also facilitate protein interactions with the mobile lipids and thus increase the protein internal motions. We speculate that the large mobility of the membrane-bound colicin Ia channel domain is a prerequisite for channel opening in the presence of a voltage gradient.

PMID: 11412120 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. J Phys Chem B. 2011 Jun 13; Authors: Ikeda K, Kameda T, Harada E, Akutsu H, Fujiwara T We report an approach to determining membrane-peptides and -protein complex structures by...	nmrlearner	Journal club	0	06-15-2011 01:15 PM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin. Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin. Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin. Proc Natl Acad Sci U S A. 2011 Apr 28; Authors: Struts AV, Salgado GF, Brown MF Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state (2)H NMR relaxation...	nmrlearner	Journal club	0	04-30-2011 12:36 PM
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation. Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation. Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation. Biophys J. 2010 Nov 17;99(10):3282-9 Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...	nmrlearner	Journal club	0	03-03-2011 12:34 PM
Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR. Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR. Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR. Protein Sci. 2011 Feb 22; Authors: Hong M, Su Y Many membrane peptides and protein domains contain functionally important cationic Arg and Lys residues, whose insertion into the hydrophobic interior of the lipid bilayer encounters significant energy barriers. To understand how these cationic molecules overcome the free energy barrier to insert into the...	nmrlearner	Journal club	0	02-24-2011 11:04 AM
[NMR paper] Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. Related Articles Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy. J Am Chem Soc. 2005 Sep 21;127(37):12965-74 Authors: Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments...	nmrlearner	Journal club	0	12-01-2010 06:56 PM
[NMR paper] Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR. Related Articles Investigation of the dynamics of an elastin-mimetic polypeptide using solid-state NMR. Magn Reson Chem. 2004 Feb;42(2):267-75 Authors: Yao XL, Conticello VP, Hong M Elastin is the main structural protein that provides elasticity to various tissues and organs in vertebrates. Molecular motions are believed to play a significant role in its elasticity. We have used solid-state NMR spectroscopy to characterize the dynamics of an elastin-mimetic...	nmrlearner	Journal club	0	11-24-2010 09:25 PM
[NMR paper] Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers. Related Articles Solid-state NMR studies of the membrane-bound closed state of the colicin E1 channel domain in lipid bilayers. Protein Sci. 1998 Feb;7(2):342-8 Authors: Kim Y, Valentine K, Opella SJ, Schendel SL, Cramer WA The colicin E1 channel polypeptide was shown to be organized anisotropically in membranes by solid-state NMR analysis of samples of uniformly 15N-labeled protein in oriented planar phospholipid bilayers. The 190...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] Membrane structure and dynamics as viewed by solid-state NMR spectroscopy. Membrane structure and dynamics as viewed by solid-state NMR spectroscopy. Related Articles Membrane structure and dynamics as viewed by solid-state NMR spectroscopy. Biophys Chem. 1997 Oct;68(1-3):233-41 Authors: Auger M The purpose of the present study is the investigation of the structure and dynamics of biological membranes using solid-state nuclear magnetic resonance (NMR) spectroscopy. Two approaches are used in our laboratory. The first involves the measurement of high-resolution 13C and 1H spectra obtained by the magic angle spinning...	nmrlearner	Journal club	0	08-22-2010 05:08 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