NMR paper Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote

		BioNMR > Educational resources > Journal club
[NMR paper] Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote

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

11-24-2010, 08:58 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

Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor prote

Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.

Related Articles Activity and NMR structure of synthetic peptides of the bovine ATPase inhibitor protein, IF1.

Peptides. 2002 Dec;23(12):2127-41

Authors: de Chiara C, Nicastro G, Spisni A, Zanotti F, Cocco T, Papa S

The protein IF(1) is a natural inhibitor of the mitochondrial F(o)F(1)-ATPase. Many investigators have been prompted to identify the shortest segment of IF(1), retaining its native activity, for use in biomedical applications. Here, the activity of the synthetic peptides IF(1)-(42-58) and IF(1)-(22-46) is correlated to their structure and conformational plasticity determined by CD and [1H]-NMR spectroscopy. Among all the IF(1) segments tested, IF(1)-(42-58) exerts the most potent, pH and temperature dependent activity on the F(o)F(1) complex. The results suggest that, due to its flexible structure, it can fold in helical and/or beta-spiral arrangements that favor the binding to the F(o)F(1) complex, where the native IF(1) binds. IF(1)-(22-46), instead, as it adopts a rigid alpha-helical conformation, it inhibits ATP hydrolysis only in the soluble F(1) moiety.

PMID: 12535691 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations. Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations. Antimicrobial peptides and their superior fluorinated analogues: structure-activity relationships as revealed by NMR spectroscopy and MD calculations. Chembiochem. 2010 Nov 22;11(17):2424-32 Authors: Díaz MD, Palomino-Schätzlein M, Corzana F, Andreu C, Carbajo RJ, del Olmo M, Canales-Mayordomo A, Pineda-Lucena A, Asensio G, Jiménez-Barbero J The conformations of two synthetic pentapeptides with...	nmrlearner	Journal club	0	05-04-2011 04:14 PM
[NMR paper] NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal u NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability. Related Articles NMR structures of two variants of bovine pancreatic trypsin inhibitor (BPTI) reveal unexpected influence of mutations on protein structure and stability. J Mol Biol. 2002 Aug 23;321(4):647-58 Authors: Cierpicki T, Otlewski J Here we determined NMR solution structures of two mutants of bovine pancreatic trypsin inhibitor (BPTI) to reveal structural reasons of their decreased...	nmrlearner	Journal club	0	11-24-2010 08:58 PM
[NMR paper] Characterization of the interaction between bovine pancreatic trypsin inhibitor and t Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR. Related Articles Characterization of the interaction between bovine pancreatic trypsin inhibitor and thiocyanate by NMR. Biophys Chem. 1998 Apr 20;71(2-3):221-34 Authors: Jolivalt C, Böckmann A, Riès-Kautt M, Ducruix A, Guittet E The interaction between Bovine Pancreatic Trypsin Inhibitor and thiocyanate was studied using NMR spectroscopy following several experimental approaches. The chemical shift variations of the BPTI protons in the...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics. Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics. J Pept Res. 1997 Mar;49(3):210-20 Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent pro Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics. Related Articles Solution structure of synthetic peptide inhibitor and substrate of cAMP-dependent protein kinase. A study by 2D H NMR and molecular dynamics. J Pept Res. 1997 Mar;49(3):210-20 Authors: Padilla A, Hauer JA, Tsigelny I, Parello J, Taylor SS Peptides derived from the inhibitor of cAMP-dependent protein kinase. PKI, have been studied by 2D 1H NMR techniques. These include the inhibitor...	nmrlearner	Journal club	0	08-22-2010 03:03 PM
[NMR paper] NMR and circular dichroism studies of synthetic peptides derived from the third intra NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR and circular dichroism studies of synthetic peptides derived from the third intracellular loop of the beta-adrenoceptor. FEBS Lett. 1995 Jan 23;358(2):133-6 Authors: Jung H, Windhaber R, Palm D, Schnackerz KD The C-terminal part of the third intracellular loop of the beta-adrenoceptor is capable...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] Conformational preferences of synthetic peptides derived from the immunodominant site Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR. Related Articles Conformational preferences of synthetic peptides derived from the immunodominant site of the circumsporozoite protein of Plasmodium falciparum by 1H NMR. Biochemistry. 1990 Aug 28;29(34):7828-37 Authors: Dyson HJ, Satterthwait AC, Lerner RA, Wright PE Proton nuclear magnetic resonance and ultraviolet circular dichroism spectroscopy have been used to probe the conformational...	nmrlearner	Journal club	0	08-21-2010 11:04 PM
1H-13C Separated Local Field Spectroscopy of Uniformly 13C Labeled Peptides and Prote 1H-13C Separated Local Field Spectroscopy of Uniformly 13C Labeled Peptides and Proteins Publication year: 2010 Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 1 July 2010</br> Eugene C., Lin , Chin H., Wu , Yuan, Yang , Christopher V., Grant , Stanley J., Opella</br> By incorporating homonuclear decoupling on both the 1H and 13C channels it is feasible to obtain high-resolution two-dimensional separated local field spectra of peptides and proteins that are 100% labeled with 13C. Dual-PISEMO (Polarization Inversion Spin Exchange Modulated...	nmrlearner	Journal club	0	08-16-2010 03:50 AM

« 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