Question from NMRWiki Q&A forum Chemical exchange of Tyr residues - what information can be found about dynamics?

		BioNMR > NMR community > News from other NMR forums
[Question from NMRWiki Q&A forum] Chemical exchange of Tyr residues - what information can be found about dynamics?

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:

View First Unread

Thread Tools

Search this Thread

Rate Thread

Display Modes

04-11-2011, 12:48 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,185

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

Chemical exchange of Tyr residues - what information can be found about dynamics?

Chemical exchange of Tyr residues - what information can be found about dynamics?

I have an aromatic spectrum of Tyr residues in p53 DNA binding domain. No peaks are seen for Tyr-205 at high temp, but as temp decreases 4 peaks are shown. Tyr-163 and Tyr-236 show two peak each at high temps. How come there aren't 4 peaks? The dynamic processes are said to occur on different time scales. What is the interpretation of this information? How is the core domain of p53 influenced by this? Thanks for your help!

Check if somebody has answered this question on NMRWiki QA forum

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy Longitudinal exchange: an alternative strategy towards quantification of dynamics parameters in ZZ exchange spectroscopy Abstract Longitudinal exchange experiments facilitate the quantification of the rates of interconversion between the exchanging species, along with their longitudinal relaxation rates, by analyzing the time-dependence of direct correlation and exchange cross peaks. Here we present a simple and robust alternative to this strategy, which is based on the combination of two complementary experiments, one with and one without resolving exchange cross peaks. We show that...	nmrlearner	Journal club	0	09-30-2011 08:01 PM
Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase Abstract We have developed NMR spectroscopic methods to investigate the tyrosines within Bacillus circulans xylanase (BcX). Four slowly exchanging buried tyrosine hydroxyl protons with chemical shifts between 7.5 and 12.5 ppm were found using a long-range 13C-HSQC experiment that exploits the 3JCH coupling between the ring 1HÎ· and 13CÎµ nuclei. The NMR signals from these protons were assigned via 13C-tyrosine selective labelling and a suite of scalar and 13C,15N-filtered/edited NOE...	nmrlearner	Journal club	0	09-17-2011 10:20 AM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1 NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1 http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi101896j/aop/images/medium/bi-2010-01896j_0004.gif Biochemistry DOI: 10.1021/bi101896j http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/OhiVTgV2ZTI More...	nmrlearner	Journal club	0	01-14-2011 01:59 AM
TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins TROSY-selected ZZ-exchange experiment for characterizing slow chemical exchange in large proteins Abstract A TROSY-selected ZZ-exchange experiment is described for measuring slow chemical exchange rates by monitoring the TROSY component of 15N longitudinal magnetization. Application of the proposed pulse sequence to the cadherin 8 N-terminal extracelluar domain demonstrates that enhanced sensitivity is obtained, compared to a previously described TROSY-detected ZZ-exchange sequence (Sahu et al. J Am Chem Soc 129: 13232â??13237, 2007), by preserving the TROSY effect during the mixing...	nmrlearner	Journal club	0	01-09-2011 12:46 PM
NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1. NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1. NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)2 Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1. Biochemistry. 2011 Jan 4; Authors: Parkesh R, Disney MD, Fountain M The NMR structure of an RNA with a copy of the 5'CUG/3'GUC motif found in the triplet repeating disorder myotonic dystrophy type 1 (DM1) is disclosed. The lowest energy conformation of the UU pair is a single...	nmrlearner	Journal club	0	01-06-2011 11:21 AM
[NMR paper] Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxatio Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation. Related Articles Motional dynamics of residues in a beta-hairpin peptide measured by 13C-NMR relaxation. Protein Sci. 1998 Mar;7(3):720-9 Authors: Ramirez-Alvarado M, Daragan VA, Serrano L, Mayo KH Structurally characterizing partially folded peptides is problematic given the nature of their transient conformational states. 13C-NMR relaxation data can provide information on the geometry of bond rotations, motional restrictions, and correlated bond rotations...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] High-resolution 13C NMR study of the topography and dynamics of methionine residues i High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin. Related Articles High-resolution 13C NMR study of the topography and dynamics of methionine residues in detergent-solubilized bacteriorhodopsin. Biochemistry. 1991 Apr 23;30(16):3885-92 Authors: Seigneuret M, Neumann JM, Levy D, Rigaud JL The proton transport membrane protein bacteriorhodopsin has been biosynthetically labeled with methionine and studied by high-resolution 13C NMR after solubilization in the detergent...	nmrlearner	Journal club	0	08-21-2010 11:16 PM
Analysis of and chemical shifts of cysteine and cystine residues in proteins: a quant Abstract Cysteines possess a unique property among the 20 naturally occurring amino acids: it can be present in proteins in either the reduced or oxidized form, and can regulate the activity of some proteins. Consequently, to augment our previous treatment of the other types of residues, the 13\textC\upalpha and 13\textC\upbeta chemical shifts of 837 cysteines in disulfide-bonded cystine from a set of seven non-redundant proteins, determined by X-ray crystallography and NMR spectroscopy, were computed at the DFT level of theory. Our results indicate that the errors between observed...	nmrlearner	Journal club	0	08-14-2010 04:19 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