NMR paper Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximatel

		BioNMR > Educational resources > Journal club
[NMR paper] Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximatel

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, 11:12 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

Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximatel

Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximately 48-kDa insulin receptor protein-tyrosine kinase results in slower rates of diphosphorylation of a series of dodecapeptide substrates. An assessment by 1H NMR.

Related Articles Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximately 48-kDa insulin receptor protein-tyrosine kinase results in slower rates of diphosphorylation of a series of dodecapeptide substrates. An assessment by 1H NMR.

J Biol Chem. 1991 Jul 5;266(19):12369-71

Authors: Levine BA, Ellis L

Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase is accompanied by an increase in its specific activity towards exogenous substrates. In the present study, we have utilized 1H NMR to compare the order and rate of mono- and diphosphorylation of multiple tyrosine residues in a series of synthetic dodecapeptide substrates (based on the receptor sequence, which includes major sites of autophosphorylation (RRDIYETDYYRK), with substitution(s) at positions 6 and/or 7 based on residue size and/or charge) by the approximately 48-kDa enzyme and by a approximately 38-kDa enzyme generated by tryptic deletion of approximately 10 kDa from the carboxyl terminus of the approximately 48-kDa protein. Both enzymes exhibit a marked order and progression of phosphorylation of peptide tyrosine residues; for each peptide, phosphorylation initiates and proceeds to completion first on tyrosine 9, followed by phosphorylation on tyrosine 10. Although removal of the carboxyl terminus does not affect the rate of monophosphorylation of these peptides on tyrosine 9, the smaller enzyme exhibits a slower rate of diphosphorylation (at tyrosine 10), as compared with the approximately 48-kDa enzyme.

PMID: 1648094 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
TROSY NMR Spectroscopy of Large Soluble Proteins. TROSY NMR Spectroscopy of Large Soluble Proteins. TROSY NMR Spectroscopy of Large Soluble Proteins. Top Curr Chem. 2011 Sep 17; Authors: Xu Y, Matthews S Abstract Solution nuclear magnetic resonance spectroscopy is usually only used to study proteins with molecular weight not exceeding about 50 kDa. This size limit has been lifted significantly in recent years, thanks to the development of labelling methods and the application of transverse-relaxation optimized spectroscopy (TROSY). In particular, methyl-specific labelling and...	nmrlearner	Journal club	0	09-20-2011 03:10 PM
[NMR paper] Motion of carboxyl terminus of Galpha is restricted upon G protein activation. A solu Motion of carboxyl terminus of Galpha is restricted upon G protein activation. A solution NMR study using semisynthetic Galpha subunits. Related Articles Motion of carboxyl terminus of Galpha is restricted upon G protein activation. A solution NMR study using semisynthetic Galpha subunits. J Biol Chem. 2005 Sep 2;280(35):31019-26 Authors: Anderson LL, Marshall GR, Crocker E, Smith SO, Baranski TJ The carboxyl terminus of the G protein alpha subunit plays a key role in interactions with G protein-coupled receptors. Previous studies that have...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] NMR studies on the solution structure of a deletion mutant of the transcarboxylase bi NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit. Related Articles NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit. Int J Biol Macromol. 2002 Oct 1;30(5):233-42 Authors: Jank MM, Sadowsky JD, Peikert C, Berger S A deletion mutant of the transcarboxylase biotin carrier protein was completely labeled with 13C and 15N. A multitude of 2D and 3D NMR spectra were recorded and assigned. An NMR solution structure was derived from the data...	nmrlearner	Journal club	0	11-24-2010 08:58 PM
[NMR paper] Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alp Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein. Related Articles Solution NMR structure and folding dynamics of the N terminus of a rat non-muscle alpha-tropomyosin in an engineered chimeric protein. J Mol Biol. 2001 Sep 28;312(4):833-47 Authors: Greenfield NJ, Huang YJ, Palm T, Swapna GV, Monleon D, Montelione GT, Hitchcock-DeGregori SE Tropomyosin is an alpha-helical coiled-coil protein that aligns head-to-tail along the length of the actin filament and...	nmrlearner	Journal club	0	11-19-2010 08:44 PM
[NMR paper] Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus ac Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin. Related Articles Solution (1)H NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin. J Biol Chem. 2000 Jan 14;275(2):742-51 Authors: Nguyen BD, Xia Z, Cutruzzolá F, Allocatelli CT, Brunori M, La Mar GN The sea hare Aplysia limacina...	nmrlearner	Journal club	0	11-18-2010 09:15 PM
[NMR paper] NMR structure and functional characteristics of the hydrophilic N terminus of the pot NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. Related Articles NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1. J Biol Chem. 1999 Dec 10;274(50):35521-5 Authors: Wissmann R, Baukrowitz T, Kalbacher H, Kalbitzer HR, Ruppersberg JP, Pongs O, Antz C, Fakler B Rapid N-type inactivation of voltage-dependent potassium (Kv) channels controls membrane excitability and signal propagation in central...	nmrlearner	Journal club	0	11-18-2010 08:31 PM
[NMR paper] Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximatel Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximately 48-kDa insulin receptor protein-tyrosine kinase results in slower rates of diphosphorylation of a series of dodecapeptide substrates. An assessment by 1H NMR. Related Articles Deletion of approximately 10 kDa from the carboxyl terminus of a soluble approximately 48-kDa insulin receptor protein-tyrosine kinase results in slower rates of diphosphorylation of a series of dodecapeptide substrates. An assessment by 1H NMR. J Biol Chem. 1991 Jul 5;266(19):12369-71 Authors: ...	nmrlearner	Journal club	0	08-21-2010 11:12 PM
[NMR paper] Solution structure of the carboxyl terminus of a human class Mu glutathione S-transfe Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structure of the carboxyl terminus of a human class Mu glutathione S-transferase: NMR assignment strategies in large proteins. J Mol Biol. 1999 Feb 5;285(5):2119-32 Authors: McCallum SA, Hitchens TK, Rule GS Strategies to obtain the NMR assignments for the HN, N, CO, Calpha and...	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