NMR paper Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectrosc

		BioNMR > Educational resources > Journal club
[NMR paper] Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectrosc

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, 03:29 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,732

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

Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectrosc

Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectroscopy.

Related Articles Structure and dynamics of tosylchymotrypsin at pH 7 examined by tritium NMR spectroscopy.

Biochim Biophys Acta. 1994 Sep 21;1208(1):171-8

Authors: O'Connell TM, Gerig JT, Williams PG

3H-NMR spectroscopy of specifically tritiated and tritiated/deuterated derivatives of tosylchymotrypsin has been used to examine the behavior of the tosyl group in this protein at pH 7. The presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of T1 relaxation, line widths, and various nuclear Overhauser experiments for the collection of tritiated species present in the samples were used to the interpret the observations made. These analyses suggests that the tosyl group of tosylchymotrypsin at pH 7 is largely retained within the substrate specificity pocket observed in the crystal structure. This outcome is in strong contrast to the situation observed at pH 4, where the tosyl group is mobile enough to be found outside the specificity pocket an appreciable fraction of the time, and may be the result of protein association at pH 7.

PMID: 8086432 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Reconstitution of a native-like SH2 domain from disordered peptide fragments examined Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR. Related Articles Reconstitution of a native-like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR. Protein Sci. 2001 Nov;10(11):2162-75 Authors: Ojennus DD, Fleissner MR, Wuttke DS The N-terminal SH2 domain from the p85alpha subunit of phosphatidylinositol 3' kinase is cleaved specifically into 9- and 5-kD fragments by limited proteolytic digestion with trypsin. The noncovalent...	nmrlearner	Journal club	0	11-19-2010 08:44 PM
[NMR paper] Evidence of secondary structure by high-resolution magic angle spinning NMR spectrosc Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports. Related Articles Evidence of secondary structure by high-resolution magic angle spinning NMR spectroscopy of a bioactive peptide bound to different solid supports. J Am Chem Soc. 2001 May 9;123(18):4130-8 Authors: Furrer J, Piotto M, Bourdonneau M, Limal D, Guichard G, Elbayed K, Raya J, Briand JP, Bianco A The structure of the 19-amino acid peptide epitope, corresponding to the 141-159 sequence of...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectrosc Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy. Related Articles Structure of the metal-water complex in Ras x GDP studied by high-field EPR spectroscopy and 31P NMR spectroscopy. Biochemistry. 2001 Feb 20;40(7):1884-9 Authors: Rohrer M, Prisner TF, Brügmann O, Käss H, Spoerner M, Wittinghofer A, Kalbitzer HR The small GTPase Ras plays a key role as a molecular switch in the intercellular signal transduction. On Mg(2+) --> Mn(2+) substituted samples, the first ligand sphere of...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectrosc Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy. Related Articles Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy. Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):421-4 Authors: Vivian JP, Wilce JA, Hastings AF, Wilce MC The replication terminator protein (RTP)-DNA complex of Bacillus subtilis is responsible for the arrest of DNA replication at terminator sites in the B. subtilis chromosome. The crystallization and preliminary diffraction data analysis...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Microscopic stability of cold shock protein A examined by NMR native state hydrogen e Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide. Related Articles Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxide. Protein Sci. 2000 Feb;9(2):290-301 Authors: Jaravine VA, Rathgeb-Szabo K, Alexandrescu AT Native state hydrogen exchange of cold shock protein A (CspA) has been characterized as a function of the denaturant urea and of the stabilizing agent...	nmrlearner	Journal club	0	11-18-2010 09:15 PM
[NMR paper] Identification of cysteine ligands in metalloproteins using optical and NMR spectrosc Identification of cysteine ligands in metalloproteins using optical and NMR spectroscopy: cadmium-substituted rubredoxin as a model 2- center. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Identification of cysteine ligands in metalloproteins using optical and NMR spectroscopy: cadmium-substituted rubredoxin as a model 2- center. Protein...	nmrlearner	Journal club	0	08-22-2010 03:01 AM
[NMR paper] Tritium NMR spectroscopy of ligand binding to maltose-binding protein. Tritium NMR spectroscopy of ligand binding to maltose-binding protein. Related Articles Tritium NMR spectroscopy of ligand binding to maltose-binding protein. Biochemistry. 1991 Jun 4;30(22):5524-31 Authors: Gehring K, Williams PG, Pelton JG, Morimoto H, Wemmer DE Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied. Tritium NMR spectroscopy...	nmrlearner	Journal club	0	08-21-2010 11:16 PM
[NMR paper] Structural characterization of peptide hormone/receptor interactions by NMR spectrosc Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Structural characterization of peptide hormone/receptor interactions by NMR spectroscopy. Biopolymers. 1999;51(3):208-20 Authors: Pellegrini M, Mierke DF The structural characterization of peptide hormones and their interaction with G-protein (guanine nucleotide-binding regulatory protein) coupled...	nmrlearner	Journal club	0	08-21-2010 04:03 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