NMR paper Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by

		BioNMR > Educational resources > Journal club
[NMR paper] Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by

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, 02:20 PM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,733

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

Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by

Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.

Related Articles Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.

J Biomol NMR. 1996 Dec;8(4):417-28

Authors: Sethson I, Edlund U, Holak TA, Ross A, Jonsson BH

The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of the largest monomeric proteins assigned so far. The assignment was enabled by a combination of 3D triple-resonance experiments and extensive use of amino acid-specific 15N-labeling. The obtained resonance assignment has been used to evaluate the secondary structure elements present in solution. The solution structure appears to be very similar to the crystal structure, although some differences can be observed. Proton-deuteron exchange experiments have shown that the assignments provide probes that can be used in future studies of HCA I.

PMID: 9008361 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR Intrinsic Proton-Donating Power of Zinc-Bound Water in a Carbonic Anhydrase Active Site Model Estimated by NMR Stepan B. Lesnichin, Ilya G. Shenderovich, Titin Muljati, David Silverman and Hans-Heinrich Limbach http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja203478j/aop/images/medium/ja-2011-03478j_0004.gif Journal of the American Chemical Society DOI: 10.1021/ja203478j http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/pgOKoZytT3U	nmrlearner	Journal club	0	07-02-2011 05:30 AM
[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] Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human cal Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy. Related Articles Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy. Protein Sci. 1998 Nov;7(11):2421-30 Authors: Qian H, Rogers MS, Schleucher J, Edlund U, Strehler EE, Sethson I Human calmodulin-like protein (CLP) is closely related to vertebrate calmodulin, yet its unique cell specific expression pattern, overlapping but...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a dou Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Assignment of the backbone 1H,15N,13C NMR resonances and secondary structure of a double-stranded RNA binding domain from the Drosophila protein staufen. FEBS Lett. 1995 Apr 10;362(3):333-6 Authors: Bycroft M, Proctor M, Freund SM, St Johnston D NMR spectroscopy has been...	nmrlearner	Journal club	0	08-22-2010 03:41 AM
[NMR paper] Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronucle Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronuclear NMR spectroscopy at natural abundance. Related Articles Assignment of the protonated 13C resonances of apo-neocarzinostatin by 2D heteronuclear NMR spectroscopy at natural abundance. J Biomol NMR. 1994 Sep;4(5):689-702 Authors: Lefevre C, Adjadj E, Quiniou E, Mispelter J Nearly complete assignment of the protonated carbon resonances of apo-neocarzinostatin, a 113-amino acid antitumor antibiotic carrier protein, has been achieved at natural 13C abundance...	nmrlearner	Journal club	0	08-22-2010 03:29 AM
[NMR paper] The interaction of acetate and formate with cobalt carbonic anhydrase. An NMR study. The interaction of acetate and formate with cobalt carbonic anhydrase. An NMR study. 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 The interaction of acetate and formate with cobalt carbonic anhydrase. An NMR study. Eur J Biochem. 1992 Sep 15;208(3):607-15 Authors: Bertini I, Luchinat C, Pierattelli R, Vila AJ The interaction of formate and acetate ions with cobalt-substituted carbonic anhydrase (CA) has been investigated...	nmrlearner	Journal club	0	08-21-2010 11:45 PM
[NMR paper] Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites. FEBS Lett. 1999 Feb 26;445(2-3):361-5 Authors: Jonasson P, Kjellsson A, Sethson I, Jonsson BH Hydrogen/deuterium (H/D) exchange measurements in low and moderate...	nmrlearner	Journal club	0	08-21-2010 04:03 PM
Approaches to the assignment of 19F resonances from 3-fluorophenylalanine labeled cal Abstract Traditional single site replacement mutations (in this case, phenylalanine to tyrosine) were compared with methods which exclusively employ 15N and 19F-edited two- and three-dimensional NMR experiments for purposes of assigning 19F NMR resonances from calmodulin (CaM), biosynthetically labeled with 3-fluorophenylalanine (3-FPhe). The global substitution of 3-FPhe for native phenylalanine was tolerated in CaM as evidenced by a comparison of 1H-15N HSQC spectra and calcium binding assays in the presence and absence of 3-FPhe. The 19F NMR spectrum reveals six resolved resonances, one...	nmrlearner	Journal club	0	08-14-2010 04:19 AM

« 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