NMR paper Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural diffe

		BioNMR > Educational resources > Journal club
[NMR paper] Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural diffe

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

08-21-2010, 10:48 PM

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

Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural diffe

Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural differences. A 1H and 15N NMR study.

Related Articles Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 shows dynamic not structural differences. A 1H and 15N NMR study.

FEBS Lett. 1990 Jan 29;260(2):225-8

Authors: Gooley PR, MacKenzie NE

Comparative analysis of nuclear Overhauser effects show that the time average conformation of the wild-type and mutant Pro----Ala-35 Rhodobacter capsulatus cytochrome c2 are indistinguishable. The ring resonances of Phe-51 and Tyr-53 show that their ring flip rates increase in P35A. NH proton exchange studies show that the exchange rates of the NH of Gly-34 and the NpiH of His-17 increase by approximately 10(2) in P35A suggesting that their respective hydrogen bonds are destabilized in this protein. However, 3JchiNH 1H and 15N chemical shift data argue that these bonds are intact. These data are compatible if the replacement of a Pro with an Ala residue forms a cavity or increases local flexibility thus reducing steric hinderance and increasing solvent accessibility.

PMID: 2153585 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Structural biology: Proteins in dynamic equilibrium - Nature.com Structural biology: Proteins in dynamic equilibrium - Nature.com <img alt="" height="1" width="1" /> Structural biology: Proteins in dynamic equilibrium Nature.com Changes in global orientations of protein domains, or in the shape and size of molecular assemblies, are more difficult to characterize using NMR alone, ... Read here	nmrlearner	Online News	0	12-23-2010 02:43 AM
[NMR paper] The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 vis The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK. Related Articles The orientations of cytochrome c in the highly dynamic complex with cytochrome b5 visualized by NMR and docking using HADDOCK. Protein Sci. 2005 Mar;14(3):799-811 Authors: Volkov AN, Ferrari D, Worrall JA, Bonvin AM, Ubbink M The interaction of bovine microsomal ferricytochrome b5 with yeast iso-1-ferri and ferrocytochrome c has been investigated using heteronuclear NMR techniques. Chemical-shift...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] (1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamba (1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles. Related Articles (1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles. Biophys J. 2004 Aug;87(2):1205-14 Authors: Metcalfe EE, Zamoon J, Thomas DD, Veglia G We report the backbone dynamics of monomeric phospholamban in dodecylphosphocholine micelles using (1)H/(15)N heteronuclear NMR spectroscopy. Phospholamban is a 52-amino acid...	nmrlearner	Journal club	0	11-24-2010 10:01 PM
[NMR paper] NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure. Related Articles NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure. J Biol Chem. 2004 Apr 9;279(15):15177-82 Authors: Wain R, Redfield C, Ferguson SJ, Smith LJ Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein...	nmrlearner	Journal club	0	11-24-2010 09:25 PM
[NMR paper] Structural and dynamic characterization of the phosphotyrosine binding region of a Sr Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches. Related Articles Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches. Biochemistry. 1995 Sep 12;34(36):11353-62 Authors: Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD Arginine side chains are often...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] NMR assignment of Rhodobacter capsulatus ferricytochrome c', a 28 kDa paramagnetic he NMR assignment of Rhodobacter capsulatus ferricytochrome c', a 28 kDa paramagnetic heme protein. Related Articles NMR assignment of Rhodobacter capsulatus ferricytochrome c', a 28 kDa paramagnetic heme protein. Biochemistry. 1995 May 2;34(17):5904-12 Authors: Caffrey M, Simorre JP, Brutscher B, Cusanovich M, Marion D The cytochromes c' are paramagnetic heme proteins generally consisting of two identical 14 kDa subunits. The 1H and 15N resonances of the ferricytochrome c' from the purple phototrophic bacterium Rhodobacter capsulatus have been...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cy Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study. Related Articles Comparison of amide proton exchange in reduced and oxidized Rhodobacter capsulatus cytochrome c2: a 1H-15N NMR study. J Biomol NMR. 1991 Jul;1(2):145-54 Authors: Gooley PR, Zhao D, MacKenzie NE The hydrogen-deuterium exchange rates of the reduced and oxidized forms of Rhodobacter capsulatus cytochrome c2 were studied by 1H-15N homonuclear multiple quantum correlation spectroscopy. Minimal differences were...	nmrlearner	Journal club	0	08-21-2010 11:16 PM
[NMR paper] Assignment of the 1H and 15N NMR spectra of Rhodobacter capsulatus ferrocytochrome c2 Assignment of the 1H and 15N NMR spectra of Rhodobacter capsulatus ferrocytochrome c2. Related Articles Assignment of the 1H and 15N NMR spectra of Rhodobacter capsulatus ferrocytochrome c2. Biochemistry. 1990 Mar 6;29(9):2278-90 Authors: Gooley PR, Caffrey MS, Cusanovich MA, MacKenzie NE The peptide resonances of the 1H and 15N nuclear magnetic resonance spectra of ferrocytochrome c2 from Rhodobacter capsulatus are sequentially assigned by a combination of 2D 1H-1H and 1H-15N spectroscopy, the latter performed on 15N-enriched protein....	nmrlearner	Journal club	0	08-21-2010 10:48 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