NMR paper Populating the equilibrium molten globule state of apomyoglobin under conditions suit

		BioNMR > Educational resources > Journal club
[NMR paper] Populating the equilibrium molten globule state of apomyoglobin under conditions suit

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

08-22-2010, 05:08 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

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

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.

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 state of apomyoglobin is stable and remains monomeric for periods of time sufficient for the application of three-dimensional heteronuclear NMR experiments. The quality of initial two-dimensional NMR spectra suggests that sequence-specific assignments can be made for a majority of the protein resonances under these conditions. A pH titration of the protein followed using two-dimensional 1H-15N correlation experiments indicates that the equilibrium intermediate undergoes fast exchange on the chemical shift time scale with the unfolded state and intermediate time scale exchange with the native state, and suggests a strategy to assist with backbone resonance assignments. The conditions and techniques described may be applicable to the characterization of other equilibrium folding intermediates.

PMID: 9395082 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

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] 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] The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H in The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin. Related Articles The native state of apomyoglobin described by proton NMR spectroscopy: the A-B-G-H interface of wild-type sperm whale apomyoglobin. Proteins. 1996 Jul;25(3):267-85 Authors: Lecomte JT, Kao YH, Cocco MJ Proton nuclear magnetic resonance spectroscopy was applied to sperm whale apomyoglobin to describe the conformation adopted by the protein under native conditions. The study focused on the A-B-G-H...	nmrlearner	Journal club	0	08-22-2010 02:27 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 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...	nmrlearner	Journal club	0	08-21-2010 11:53 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