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 11-24-2010, 08:58 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 23,732
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 Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR.

Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.

Related Articles Study of wheat high molecular weight 1Dx5 subunit by (13)C and (1)H solid-state NMR. II. Roles of nonrepetitive terminal domains and length of repetitive domain.

Biopolymers. 2002 Oct 15;65(2):158-68

Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Naito A, Okuda K, Saitô H, Gil AM

This work follows a previous article that addressed the role of disulfide bonds in the behavior of the 1Dx5 subunit upon hydration. Here the roles of nonrepetitive terminal domains present and the length of the central repetitive domain in the hydration of 1Dx5 are investigated. This was achieved by comparing the hydration behavior of suitable model samples determined by (13)C- and (1)H-NMR: an alkylated 1Dx5 subunit (alk1Dx5), a recombinant 58-kDa peptide corresponding to the central repetitive domain of 1Dx5 (i.e., lacking the terminal domains), and two synthetic peptides (with 6 and 21 amino acid residues) based on the consensus repeat motifs of the central domain. The (13)C cross-polarization and magic angle spinning (MAS) experiments recorded as a function of hydration gave information about the protein or peptide fractions resisting plasticization. Conversely, (13)C single pulse excitation and (1)H-MAS gave information on the more plasticized segments. The results are consistent with the previous proposal of a hydrated network held by hydrogen-bonded glutamines and possibly hydrophobic interactions. The nonrepetitive terminal domains were found to induce water insolubility and a generally higher network hindrance. Shorter chain lengths were shown to increase plasticization and water solubility. However, at low water contents, the 21-mer peptide was characterized by higher hindrance in the megahertz and kilohertz frequency ranges compared to the longer peptide; and a tendency for a few hydrogen-bonded glutamines and hydrophobic residues to remain relatively hindered was still observed, as for the protein and large peptide. It is suggested that this ability is strongly dependent on the peptide primary structure.

PMID: 12209466 [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
An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins.
An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins. An optimized isotopic labelling strategy of isoleucine-?(2) methyl groups for solution NMR studies of high molecular weight proteins. Chem Commun (Camb). 2011 Jul 26; Authors: Ayala I, Hamelin O, Amero C, Pessey O, Plevin MJ, Gans P, Boisbouvier J An efficient synthetic route is proposed to produce 2-hydroxy-2-ethyl-3-oxobutanoate for the specific labelling of Ile methyl-?(2) groups in proteins. The (2)H,...
nmrlearner Journal club 0 07-28-2011 10:51 AM
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins
Alanine Methyl Groups as NMR Probes of Molecular Structure and Dynamics in High-Molecular-Weight Proteins Raquel Godoy-Ruiz, Chenyun Guo and Vitali Tugarinov http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1083656/aop/images/medium/ja-2010-083656_0009.gif Journal of the American Chemical Society DOI: 10.1021/ja1083656 http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/hxZ4cabF688
nmrlearner Journal club 0 12-08-2010 10:04 AM
[NMR paper] Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin r
Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. Related Articles Probing side-chain dynamics in high molecular weight proteins by deuterium NMR spin relaxation: an application to an 82-kDa enzyme. J Am Chem Soc. 2005 Jun 8;127(22):8214-25 Authors: Tugarinov V, Ollerenshaw JE, Kay LE New NMR experiments for the measurement of side-chain dynamics in high molecular weight ( approximately 100 kDa) proteins are presented. The experiments quantify (2)H spin...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] A solid-state NMR study of molecular mobility and phase separation in co-spray-dried
A solid-state NMR study of molecular mobility and phase separation in co-spray-dried protein-sugar particles. Related Articles A solid-state NMR study of molecular mobility and phase separation in co-spray-dried protein-sugar particles. Eur J Pharm Sci. 2005 May;25(1):105-12 Authors: Suihko EJ, Forbes RT, Apperley DC Molecular mobility and physical form of co-spray-dried sugar-lysozyme formulations were evaluated. Co-spray-dried trehalose:lysozyme and sucrose:lysozyme formulations in 1:9, 1:1 and 9:1 ratios (w:w) were stored at 0% RH and 75%...
nmrlearner Journal club 0 11-25-2010 08:21 PM
[NMR paper] Quantitative NMR studies of high molecular weight proteins: application to domain ori
Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G. Related Articles Quantitative NMR studies of high molecular weight proteins: application to domain orientation and ligand binding in the 723 residue enzyme malate synthase G. J Mol Biol. 2003 Apr 11;327(5):1121-33 Authors: Tugarinov V, Kay LE A high-resolution multidimensional NMR study of ligand-binding to Escherichia coli malate synthase G (MSG), a 723-residue monomeric enzyme (81.4...
nmrlearner Journal club 0 11-24-2010 09:01 PM
[NMR paper] Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state
Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking. Related Articles Study of high molecular weight wheat glutenin subunit 1Dx5 by 13C and 1H solid-state NMR spectroscopy. I. Role of covalent crosslinking. Biopolymers. 2002;67(6):487-98 Authors: Alberti E, Gilbert SM, Tatham AS, Shewry PR, Gil AM This work describes a carbon and proton solid-state NMR study of the hydration of a high molecular weight wheat glutenin subunit, 1Dx5. The effect of the presence of...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] Backbone NMR assignments of a high molecular weight protein (47 kDa), cyclic AMP rece
Backbone NMR assignments of a high molecular weight protein (47 kDa), cyclic AMP receptor protein (apo-CRP) Related Articles Backbone NMR assignments of a high molecular weight protein (47 kDa), cyclic AMP receptor protein (apo-CRP) J Biomol NMR. 2000 Jan;16(1):79-80 Authors: Won HS, Yamazaki T, Lee TW, Jee JG, Yoon MK, Park SH, Otomo T, Aiba H, Kyogoku Y, Lee BJ
nmrlearner Journal club 0 11-18-2010 09:15 PM
[NMR paper] A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c
A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A high-resolution solid-state 13C-NMR study on crystalline bovine heart cytochrome-c oxidase and lysozyme. Dynamic behavior of protein and detergent in the complex. Eur J Biochem. 1992 Sep 15;208(3):713-20 Authors: Tuzi S,...
nmrlearner Journal club 0 08-21-2010 11:45 PM



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 08:30 PM.


Map