NMR paper 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch

		BioNMR > Educational resources > Journal club
[NMR paper] 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch

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

08-22-2010, 03:03 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,174

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

1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch

1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.

Related Articles 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein.

Eur J Biochem. 1997 Jun 1;246(2):301-10

Authors: Beglova N, Fischer D, Hengge-Aronis R, Gehring K

GlgS is a 7892-Da protein which is involved in glycogen biosynthesis in bacteria. We report the 1H, 15N and 13C NMR assignments of the backbone and side-chain resonances at 25 degrees C and pH 6.7 from two-dimensional homonuclear and three-dimensional heteronuclear NMR experiments. The secondary structure of the protein was determined using sequential and medium-range NOE correlations, vicinal 3J(NH-H alpha) coupling values and amide proton exchange rates. The secondary structure obtained is consistent with the secondary chemical shifts of 1H alpha, 13C alpha and 13C = O. It was found that the secondary structure of GlgS comprises two amphipathic helices (Asn10-Met21 and Glu39-Arg60), one short highly hydrophobic helix (Ile30-Val33), a short extended beta-strand-like fragment (Arg26-Asp29) and two type I beta-turns (His22-Gly25 and Thr34-Met37). An overall topology of GlgS is suggested based on long-range NOEs. The elements of secondary structure form a sandwich in which the beta-strand and the short hydrophobic helix are positioned between the two amphipathic helices.

PMID: 9208918 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Esch 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. 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 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. Eur J Biochem. 1997 Jun 1;246(2):301-10 Authors: Beglova N, Fischer D, Hengge-Aronis R, Gehring K GlgS is a 7892-Da protein which is involved in glycogen...	nmrlearner	Journal club	0	08-22-2010 03:31 PM
[NMR paper] Primary structure, sequence-specific 1H-NMR assignments and secondary structure in so Primary structure, sequence-specific 1H-NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem. 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 Primary structure, sequence-specific 1H-NMR assignments and secondary structure in solution of bromelain inhibitor VI from pineapple stem. Eur J Biochem. 1995 Sep 1;232(2):335-43 Authors: Hatano K, Kojima M, Tanokura M, Takahashi K One of the...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue s Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus. Related Articles Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus. J Biomol NMR. 1995 Apr;5(3):259-70 Authors: Fogh RH, Schipper D, Boelens R, Kaptein R The 1H, 13C and 15N NMR resonances of serine protease PB92 have been assigned using 3D triple-resonance NMR techniques. With a molecular weight of 27 kDa (269 residues) this...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. J Biomol NMR. 1994 Mar;4(2):257-78 Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ 1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue p 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. Related Articles 1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus. J Biomol NMR. 1994 Mar;4(2):257-78 Authors: Remerowski ML, Domke T, Groenewegen A, Pepermans HA, Hilbers CW, van de Ven FJ 1H, 13C and 15N NMR assignments of the backbone atoms of subtilisin 309, secreted by Bacillus lentus, have been made using heteronuclear 3D NMR...	nmrlearner	Journal club	0	08-22-2010 03:33 AM
[NMR paper] 1H resonance assignments, secondary structure and general topology of single-chain mo 1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR. Related Articles 1H resonance assignments, secondary structure and general topology of single-chain monellin in solution as determined by 1H 2D-NMR. J Biomol NMR. 1992 Nov;2(6):557-72 Authors: Tomic MT, Somoza JR, Wemmer DE, Park YW, Cho JM, Kim SH We determined the resonance assignments, secondary structure and general topology of the 11-kDa sweet protein single-chain monellin (SCM), using two-dimensional proton...	nmrlearner	Journal club	0	08-21-2010 11:45 PM
[NMR paper] Secondary structure and topology of interleukin-1 receptor antagonist protein determi Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy. Related Articles Secondary structure and topology of interleukin-1 receptor antagonist protein determined by heteronuclear three-dimensional NMR spectroscopy. Biochemistry. 1992 Jun 16;31(23):5237-45 Authors: Stockman BJ, Scahill TA, Roy M, Ulrich EL, Strakalaitis NA, Brunner DP, Yem AW, Deibel MR Interleukin-1 (IL-1) proteins, such as IL-1 beta, play a key role in immune and inflammatory responses....	nmrlearner	Journal club	0	08-21-2010 11:41 PM
[NMR paper] Determination of the secondary structure and molecular topology of interleukin-1 beta Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy. Related Articles Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy. Biochemistry. 1990 May 15;29(19):4668-82 Authors: Driscoll PC, Gronenborn AM, Wingfield PT, Clore GM A study of the regular secondary structure elements of recombinant human interleukin-1 beta has been...	nmrlearner	Journal club	0	08-21-2010 10:48 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