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 08-22-2010, 03:01 AM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,578
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 Secondary structure and zinc ligation of human recombinant short-form stromelysin by

Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional heteronuclear NMR.

Related Articles Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional heteronuclear NMR.

Biochemistry. 1993 Dec 7;32(48):13098-108

Authors: Gooley PR, Johnson BA, Marcy AI, Cuca GC, Salowe SP, Hagmann WK, Esser CK, Springer JP

Stromelysin-1, a member of the matrix metalloendoprotease family, is a zinc protease involved in the degradation of connective tissue in the extracellular matrix. As a step toward determining the structure of this protein, multidimensional heteronuclear NMR experiments have been applied to an inhibited truncated form of human stromelysin-1. Extensive 1H, 13C, and 15N sequential assignments have been obtained with a combination of three- and four-dimensional experiments. On the basis of sequential and short-range NOEs and 13C alpha chemical shifts, two helices have been delineated, spanning residues Asp-111 to Val-127 and Leu-195 to Ser-206. A third helix spanning residues Asp-238 to Gly-247 is characterized by sequential NOEs and 13C alpha chemical shifts, but not short-range NOEs. The lack of the latter NOEs suggests that this helix is either distorted or mobile. Similarly, sequential and interstrand NOEs and 13C alpha chemical shifts characterize a four-stranded beta-sheet with three parallel strands (Arg-100 to Ile-101, Ile-142 to Ala-147, Asp-177 to Asp-181) and one antiparallel strand (Ala-165 to Tyr-168). Two zinc sites have been identified in stromelysin [Salowe et al. (1992) Biochemistry 31, 4535-4540]. The NMR spectral properties, including chemical shift, pH dependence, and proton coupling of the imidazole nitrogens of six histidine residues (151, 166, 179, 201, 205, and 211), invariant in the matrix metalloendoprotease family, suggest that these residues are zinc ligands. NOE data indicate that these histidines form two clusters: one ligates the catalytic zinc (His-201, -205, and -211), and the other ligates a structural zinc (His-151, -166, and -179). Heteronuclear multiple quantum correlated spectra and specific labeling experiments indicate His-151, -179, -201, -205, and -211 are in the N delta 1H tautomer and His-166 is in the N epsilon 2H tautomer.

PMID: 8241164 [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] Chemical ligation of folded recombinant proteins: segmental isotopic labeling of doma
Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Related Articles Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc Natl Acad Sci U S A. 1999 Jan 19;96(2):388-93 Authors: Xu R, Ayers B, Cowburn D, Muir TW A convenient in vitro chemical ligation strategy has been developed that allows folded recombinant proteins to be joined together. This strategy permits segmental, selective isotopic labeling of the product. The src homology...
nmrlearner Journal club 0 11-18-2010 07:05 PM
[NMR paper] Structure of recombinant human parathyroid hormone in solution using multidimensional
Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy. Related Articles Structure of recombinant human parathyroid hormone in solution using multidimensional NMR spectroscopy. Biol Chem Hoppe Seyler. 1996 Mar;377(3):175-86 Authors: Gronwald W, Schomburg D, Harder MP, Mayer H, Paulsen J, Wingender E, Wray V The solution structure of human parathyroid hormone, in the form of recombinant prolyl-hPTH(1-84), has been investigated by multidimensional NMR spectroscopy under conditions (aqueous...
nmrlearner Journal club 0 08-22-2010 02:27 PM
[NMR paper] Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2
Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. Related Articles Secondary structure and protein folding of recombinant chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii as determined by 1H NMR. J Biochem. 1993 Sep;114(3):421-31 Authors: Lancelin JM, Stein M, Jacquot JP The recombinant form of the chloroplastic thioredoxin Ch2 from the green alga Chlamydomonas reinhardtii that preferentially activates the NADP...
nmrlearner Journal club 0 08-22-2010 03:01 AM
[NMR paper] Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-d
Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain. Related Articles Sequential 1H and 15N NMR assignments and secondary structure of a recombinant anti-digoxin antibody VL domain. Biochemistry. 1992 Jun 2;31(21):5033-43 Authors: Constantine KL, Goldfarb V, Wittekind M, Anthony J, Ng SC, Mueller L A uniformly 15N-labeled recombinant light-chain variable (VL) domain from the anti-digoxin antibody 26-10 has been investigated by heteronuclear two-dimensional (2D) and three-dimensional...
nmrlearner Journal club 0 08-21-2010 11:41 PM
[NMR paper] Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure o
Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition. Related Articles Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition. Biochemistry. 1991 Apr 9;30(14):3371-86 Authors: Kochoyan M, Havel TF, Nguyen DT, Dahl CE, Keutmann HT, Weiss MA ZFY, a sex-related Zn-finger protein encoded by the human Y chromosome, is distinguished from the general...
nmrlearner Journal club 0 08-21-2010 11:16 PM
[NMR paper] Protein secondary structure determination by NMR. Application with recombinant human
Protein secondary structure determination by NMR. Application with recombinant human cyclophilin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein secondary structure determination by NMR. Application with recombinant human cyclophilin. FEBS Lett. 1991 Jul 22;285(2):237-47 Authors: Wüthrich K, Spitzfaden C, Memmert K, Widmer H, Wider G It is a unique trait of the NMR method for protein structure determination that a description of the polypeptide secondary...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] Protein secondary structure determination by NMR. Application with recombinant human
Protein secondary structure determination by NMR. Application with recombinant human cyclophilin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein secondary structure determination by NMR. Application with recombinant human cyclophilin. FEBS Lett. 1991 Jul 22;285(2):237-47 Authors: Wüthrich K, Spitzfaden C, Memmert K, Widmer H, Wider G It is a unique trait of the NMR method for protein structure determination that a description of the polypeptide secondary...
nmrlearner Journal club 0 08-21-2010 11:12 PM
[NMR paper] 1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-termin
1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X. Related Articles 1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X. Biochemistry. 1990 Sep 4;29(35):8111-8 Authors: Selander M, Persson E, Stenflo J, Drakenberg T Blood coagulation factor X is composed of discrete domains, two of which are homologous to the epidermal growth factor (EGF). The...
nmrlearner Journal club 0 08-21-2010 11:04 PM


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 07:03 AM.


Map