BioNMR
NMR aggregator & online community since 2003
BioNMR    
Learn or help to learn NMR - get free NMR books!
 

Go Back   BioNMR > Educational resources > Journal club
Advanced Search
Home Forums Wiki NMR feeds Downloads Register Today's Posts



Jobs Groups Conferences Literature Pulse sequences Software forums Programs Sample preps Web resources BioNMR issues


Webservers
NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


Reply
 
Thread Tools Search this Thread Rate Thread Display Modes
  #1  
Old 08-22-2010, 03:01 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,733
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 193,617
Downloads: 0
Uploads: 0
Default Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance ass

Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.

Related Articles Helical structure and folding of subunit c of F1F0 ATP synthase: 1H NMR resonance assignments and NOE analysis.

Biochemistry. 1993 Nov 16;32(45):12167-77

Authors: Girvin ME, Fillingame RH

Subunit c of the H(+)-transporting F1F0 ATP synthase (EC 3.6.1.34) is thought to fold across the membrane as a hairpin of two alpha-helices and function as a key component of the H(+)-translocase of F0. We report here the initial results of a structural study of purified subunit c in a chloroform-methanol-water (4:4:1) solvent mixture using standard two-dimensional NMR techniques. The spin systems of 78 of the 79 amino acid side chains have been assigned to residue type, and 44 of these have been assigned to specific residues in the sequence. Stretches of alpha-helical secondary structure were observed for Asp7-ILe26 in the first proposed transmembrane helix, and for Arg50-Ile55 and Ala67-Val78 in the second proposed transmembrane helix. Nuclear Overhauser effects (NOEs) were observed between residues at both ends of the predicted transmembrane helices. The intensities of the NOEs between helix-1 and helix-2 were not diminished by mixing of 2H-subunit c with 1H-subunit c, and therefore the NOEs must be due to intramolecular, rather than intermolecular, interactions. Hence the purified protein must fold as a hairpin in this solvent system, just as it is thought to fold in the lipid bilayer of the membrane. In native F0, dicyclohexylcarbodiimide reacts specifically with Asp61 in the second transmembrane helix of subunit c, and the rate of this reaction is reduced by substitution of Ile28 by Thr on the first transmembrane helix. The I28T substitution is shown here to alter the chemical shifts of protons at and around Asp61. This observation provides a further indication that subunit c may fold in chloroform-methanol-water solvent much like it does in the membrane.

PMID: 8218294 [PubMed - indexed for MEDLINE]



Source: PubMed
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR. Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR. J Biomol NMR. 2010 Sep;48(1):1-11 Authors: Todokoro Y, Kobayashi M, Sato T, Kawakami T, Yumen I, Aimoto S, Fujiwara T, Akutsu H The subunit c-ring of H(+)-ATP synthase (F(o) c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we...
nmrlearner Journal club 0 12-18-2010 12:00 PM
[NMR paper] Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.
Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy. Related Articles Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy. Biochemistry. 2005 Sep 6;44(35):11786-94 Authors: Wilkens S, Borchardt D, Weber J, Senior AE A critical point of interaction between F(1) and F(0) in the bacterial F(1)F(0)-ATP synthase is formed by the alpha and delta subunits. Previous work has...
nmrlearner Journal club 0 12-01-2010 06:56 PM
[NMR paper] Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p
Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging. Related Articles Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging. Protein Sci. 2005 Feb;14(2):375-86 Authors: Morellet N, Druillennec S, Lenoir C, Bouaziz S, Roques BP Gag protein oligomerization, an essential step during virus assembly, results in budding of spherical virus particles. This process is critically...
nmrlearner Journal club 0 11-24-2010 11:14 PM
[NMR paper] Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with pr
Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. Related Articles Subunit A of the E. coli ATP synthase: reconstitution and high resolution NMR with protein purified in a mixed polarity solvent. FEBS Lett. 2004 Jan 2;556(1-3):35-8 Authors: Dmitriev OY, Altendorf K, Fillingame RH Subunit a of the Escherichia coli ATP synthase, a 30 kDa integral membrane protein, was purified to homogeneity by a novel procedure incorporating selective extraction into a monophasic...
nmrlearner Journal club 0 11-24-2010 09:25 PM
[NMR paper] NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed
NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site. Related Articles NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site. Biochemistry. 2000 Dec 26;39(51):15860-9 Authors: Weber T, Schaffhausen B, Liu Y, Günther UL The N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K) has a...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] CD and NMR investigations on trifluoroethanol-induced step-wise folding of helical se
CD and NMR investigations on trifluoroethanol-induced step-wise folding of helical segment from scorpion neurotoxin. Related Articles CD and NMR investigations on trifluoroethanol-induced step-wise folding of helical segment from scorpion neurotoxin. Eur J Biochem. 1999 Sep;264(2):468-78 Authors: Khandelwal P, Seth S, Hosur RV A 14 amino acid residue peptide from the helical region of Scorpion neurotoxin has been structurally characterized using CD and NMR spectroscopy in different solvent conditions. 2,2,2-Trifluoroethanol (TFE) titration has...
nmrlearner Journal club 0 11-18-2010 08:31 PM
[NMR paper] Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique envi
Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR. Related Articles Proton-translocating carboxyl of subunit c of F1Fo H(+)-ATP synthase: the unique environment suggested by the pKa determined by 1H NMR. Biochemistry. 1995 Dec 12;34(49):16186-93 Authors: Assadi-Porter FM, Fillingame RH Subunit c of the H(+)-transporting F1Fo ATP synthase (EC 3.6.1.34) is thought to fold across the membrane as a hairpin of two alpha helices with a conserved Asp/Glu residue,...
nmrlearner Journal club 0 08-22-2010 03:50 AM
[NMR paper] Structural features of the epsilon subunit of the Escherichia coli ATP synthase deter
Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Related Articles Structural features of the epsilon subunit of the Escherichia coli ATP synthase determined by NMR spectroscopy. Nat Struct Biol. 1995 Nov;2(11):961-7 Authors: Wilkens S, Dahlquist FW, McIntosh LP, Donaldson LW, Capaldi RA The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF1F0) has been determined by two- and three-dimensional heteronuclear (13C, 15N) NMR spectroscopy. The epsilon...
nmrlearner Journal club 0 08-22-2010 03:50 AM



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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Copyright, BioNMR.com, 2003-2013
Search Engine Friendly URLs by vBSEO 3.6.0

All times are GMT. The time now is 04:04 PM.


Map