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 08-21-2010, 11:53 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,583
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 Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumi

Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.

Related Articles Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.

Biochemistry. 1993 Feb 23;32(7):1707-18

Authors: Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM

Two-dimensional 1H-NMR spectroscopy has been used to study the acid-denatured molten globule (A-state) of alpha-lactalbumin. The NMR spectra show that chemical shift dispersion is limited but significantly greater than that expected for a random coil conformation. The small chemical shift dispersion of side-chain resonances in the A-state together with line broadening associated with conformational averaging indicates that most of the long-range tertiary structure in the A-state is likely to be nonspecific. Side-chain resonances in the A-state are generally shifted somewhat upfield of random coil values; this and the observation of a large number of interresidue NOEs, however, indicate that some side-chain interactions, at least at the level of hydrophobic clustering, exist in the A-state. Analysis of NOESY spectra shows no evidence for an ordered structure for either of the two major clusters of aromatic residues which in the native structure make up part of the hydrophobic core of the helical domain of the native protein. A new aromatic cluster in the A-state which results from rearrangement of the side chains of Tyr103, Trp104, and His107 from their native state positions was, however, detected by a number of well-defined interresidue NOE effects. Similar NOE patterns are observed in a peptide corresponding to residues 101-110 of alpha-lactalbumin in trifluoroethanol, suggesting that the non-native structure in the 101-110 region of the A-state is not dependent on specific interactions with the rest of the chain. Trapping experiments indicate that amide protons from regions of the sequence which in the native state are helical are among those strongly protected from solvent exchange in the A-state; those from one of the helices (the C helix) were specifically identified. Taken together, these results reinforce a model of the A-state which has stable regions of localized secondary structure but a largely disordered tertiary structure.

PMID: 8439536 [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
[NMR paper] Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NM
Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study. Related Articles Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study. Protein Sci. 2000 Aug;9(8):1540-7 Authors: Kutyshenko VP, Cortijo M We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this protein, centering the on-resonance signals either at the methyl-proton or at the...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumi
Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study. Related Articles Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study. Biochemistry. 2000 Jan 18;39(2):372-80 Authors: Bai P, Luo L, Peng Z The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a prototype of partially folded proteins. Despite the importance of molten globules in understanding the mechanisms of protein folding and its relevance to some biological...
nmrlearner Journal club 0 11-18-2010 09:15 PM
[NMR paper] Structural characterization of the molten globule and native states of ovalbumin: a 1
Structural characterization of the molten globule and native states of ovalbumin: a 1H NMR study. Related Articles Structural characterization of the molten globule and native states of ovalbumin: a 1H NMR study. J Pept Res. 1997 Dec;50(6):465-74 Authors: Sogami M, Era S, Koseki T, Nagai N Molecular characteristics of ovalbumin (OVA) in the acidic (pD 3.08, the E-form) and neutral regions were studied by measuring effective radii, 1H NMR spectra, spin-echo 1H NMR spectra and cross-relaxation times (TIS) from irradiated to observed protein...
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] Populating the equilibrium molten globule state of apomyoglobin under conditions suit
Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR. FEBS Lett. 1997 Nov 3;417(1):92-6 Authors: Eliezer D, Jennings PA, Dyson HJ, Wright PE Conditions have been determined under which the equilibrium molten globule...
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] A residue-specific NMR view of the non-cooperative unfolding of a molten globule.
A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Related Articles A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat Struct Biol. 1997 Aug;4(8):630-4 Authors: Schulman BA, Kim PS, Dobson CM, Redfield C Molten globules are partially folded forms of proteins that are thought to be general intermediates in protein folding. Nonetheless, there is limited structural information about such species because they possess conformational heterogeneity and complex dynamical properties that...
nmrlearner Journal club 0 08-22-2010 05:08 PM
[NMR paper] Is apomyoglobin a molten globule? Structural characterization by NMR.
Is apomyoglobin a molten globule? Structural characterization by NMR. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Is apomyoglobin a molten globule? Structural characterization by NMR. J Mol Biol. 1996 Nov 8;263(4):531-8 Authors: Eliezer D, Wright PE Multi-dimensional heteronuclear NMR spectroscopy has been used to obtain structural information on isotopically labeled recombinant sperm whale apomyoglobin in the native state at pH 6.1. Assignments for backbone...
nmrlearner Journal club 0 08-22-2010 02:20 PM
[NMR paper] Stability of alpha-helices in a molten globule state of cytochrome c by hydrogen-deut
Stability of alpha-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Stability of alpha-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy. J Mol Biol. 1995 Apr 7;247(4):682-8 Authors: Kuroda Y, Endo S, Nagayama K, Wada A To distinguish between intrinsically stable helices and those...
nmrlearner Journal club 0 08-22-2010 03:41 AM
[NMR paper] Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease
Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study. Related Articles Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study. Biochemistry. 1994 Feb 8;33(5):1063-72 Authors: Alexandrescu AT, Abeygunawardana C, Shortle D A partially folded form of staphylococcal nuclease has been obtained by deleting residues 4-12 and 141-149 of the 149-residue wild-type protein. Sequence-specific NMR resonance assignments have been obtained...
nmrlearner Journal club 0 08-22-2010 03:33 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 - 2017, 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 03:27 PM.


Map