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



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  
Unread 07-16-2015, 11:21 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 19,908
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 Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.

Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.

Related Articles Exploring the Protein Folding Pathway with High-Pressure NMR: Steady-State and Kinetics Studies.

Subcell Biochem. 2015;72:261-278

Authors: Roche J, Dellarole M, Royer CA, Roumestand C

Abstract
Defining the physical-chemical determinants of protein folding and stability, under normal and pathological conditions has constituted a major subfield in biophysical chemistry for over 50 years. Although a great deal of progress has been made in recent years towards this goal, a number of important questions remain. These include characterizing the structural, thermodynamic and dynamic properties of the barriers between conformational states on the protein energy landscape, understanding the sequence dependence of folding cooperativity, defining more clearly the role of solvation in controlling protein stability and dynamics and probing the high energy thermodynamic states in the native state basin and their role in misfolding and aggregation. Fundamental to the elucidation of these questions is a complete thermodynamic parameterization of protein folding determinants. In this chapter, we describe the use of high-pressure coupled to Nuclear Magnetic Resonance (NMR) spectroscopy to reveal unprecedented details on the folding energy landscape of proteins.


PMID: 26174386 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme.
Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme. Cavity as a Source of Conformational Fluctuation and High-Energy State: High-Pressure NMR Study of a Cavity-Enlarged Mutant of T4Lysozyme. Biophys J. 2015 Jan 6;108(1):133-145 Authors: Maeno A, Sindhikara D, Hirata F, Otten R, Dahlquist FW, Yokoyama S, Akasaka K, Mulder FA, Kitahara R Abstract Although the structure, function, conformational dynamics, and controlled thermodynamics of proteins...
nmrlearner Journal club 0 01-08-2015 01:29 PM
[NMR paper] Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1.
Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1. Related Articles Solution and high-pressure NMR studies of the structure, dynamics and stability of the cross-reactive allergenic cod parvalbumin Gad m 1. Proteins. 2014 Aug 12; Authors: Moraes AH, Ackerbauer D, Kostadinova M, Bublin M, de Oliveira GA, Ferreira F, Almeida FC, Breiteneder H, Valente AP Abstract Beta-parvalbumins from different fish species have been identified as the main...
nmrlearner Journal club 0 08-15-2014 12:53 PM
Protein Folding Kinetics Database
Protein Folding Kinetics Database Protein Folding Kinetics Database More...
nmrlearner General 0 05-03-2014 10:42 PM
[NMR paper] Kinase in Motion: Insights into the Dynamic Nature of p38? by High-Pressure NMR Spectroscopic Studies.
Kinase in Motion: Insights into the Dynamic Nature of p38? by High-Pressure NMR Spectroscopic Studies. Kinase in Motion: Insights into the Dynamic Nature of p38? by High-Pressure NMR Spectroscopic Studies. Chembiochem. 2013 Jul 10; Authors: Nielsen G, Jonker HR, Vajpai N, Grzesiek S, Schwalbe H Abstract Protein kinases are highly dynamic and complex molecules. Here we present high-pressure and relaxation studies of the activated p38? mitogen-activated protein kinase (MAPK). p38? plays a central role in inflammatory diseases such as...
nmrlearner Journal club 0 07-12-2013 06:01 PM
[NMR paper] Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein.
Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein. Related Articles Impact of Hydrostatic Pressure on an Intrinsically Disordered Protein: A High-Pressure NMR Study of ?-Synuclein. Chembiochem. 2013 Jun 28; Authors: Roche J, Ying J, Maltsev AS, Bax A Abstract The impact of pressure on the backbone (15) N, (1) H and (13) C chemical shifts in N-terminally acetylated ?-synuclein has been evaluated over a pressure range 1-2500 bar. Even while the chemical shifts fall very close...
nmrlearner Journal club 0 07-03-2013 01:46 PM
[NMR paper] High-pressure NMR spectroscopy for characterizing folding intermediates and denatured
High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Related Articles High-pressure NMR spectroscopy for characterizing folding intermediates and denatured states of proteins. Methods. 2004 Sep;34(1):133-43 Authors: Kamatari YO, Kitahara R, Yamada H, Yokoyama S, Akasaka K Extensive structural studies using high-pressure NMR spectroscopy have recently been carried out on proteins, which potentially contribute to our understanding of the mechanisms of protein folding. Pressure shifts the...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic c
Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using 19F NMR. Related Articles Role of entropy in protein thermostability: folding kinetics of a hyperthermophilic cold shock protein at high temperatures using 19F NMR. Biochemistry. 2002 Oct 1;41(39):11670-80 Authors: Schuler B, Kremer W, Kalbitzer HR, Jaenicke R We used (19)F NMR to extend the temperature range accessible to detailed kinetic and equilibrium studies of a hyperthermophilic protein. Employing an...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H
Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state. Proc Natl Acad Sci U S A. 1994 Sep 27;91(20):9412-6 Authors: Arcus VL, Vuilleumier S, Freund SM, Bycroft M, Fersht AR The structures of the major folding...
nmrlearner Journal club 0 08-22-2010 03:29 AM


Thread Tools Search this Thread
Search this Thread:

Advanced Search
Display Modes Rate This Thread
Rate This 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



BioNMR advertisements to pay for website hosting and domain registration. Nobody does it for us.



Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2020, 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 04:23 PM.


Map