NMR paper Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w

		BioNMR > Educational resources > Journal club
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w

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

11-24-2010, 09:16 PM

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

Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w

Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.

Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.

Biochemistry. 2003 Sep 30;42(38):11100-8

Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER

The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic resonance experiments. Distinct differences between the two states of the protein were observed. According to our data, the apo form interacts more extensively with solvent than the peptide-bound form. Significantly, the open hydrophobic substrate binding cleft of DnaK in the apo form is found to contain several molecules of water which are displaced by the binding of the hydrophobic substrate, the peptide NRLLLTG. The solvent in the hydrophobic cleft has a residence time longer than 400 ps. It is predicted that the displacement of this trapped water must contribute to the binding free energy of the natural hydrophobic substrates of this class of protein-folding chaperone proteins.

PMID: 14503860 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy Probing the Interaction of Cisplatin with the Human Copper Chaperone Atox1 by Solution and In-Cell NMR Spectroscopy Fabio Arnesano, Lucia Banci, Ivano Bertini, Isabella C. Felli, Maurizio Losacco and Giovanni Natile http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207346p/aop/images/medium/ja-2011-07346p_0003.gif Journal of the American Chemical Society DOI: 10.1021/ja207346p http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/jacsat/~4/9nWkAzWuq20	nmrlearner	Journal club	0	10-24-2011 11:06 PM
Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net Biochemists reveal interaction between tumor suppressor protein and chaperone - News-Medical.net <img alt="" height="1" width="1" /> Biochemists reveal interaction between tumor suppressor protein and chaperone News-Medical.net Using nuclear magnetic resonance (NMR) spectroscopy, the scientists at the Bavarian NMR Center in Garching were able for the first time to characterize the interaction surfaces between Hsp90 and p53 and show that p53 binds to Hsp90 in an already ... Read here	nmrlearner	Online News	0	09-08-2011 08:24 AM
[NMR paper] NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone. Related Articles NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone. J Mol Biol. 2005 May 27;349(1):163-83 Authors: Revington M, Zhang Y, Yip GN, Kurochkin AV, Zuiderweg ER Hsp70 chaperones are two-domain proteins that assist in intra-cellular protein (re) folding processes in all species. The protein folding activity of the substrate binding domain of the Hsp70s is regulated by...	nmrlearner	Journal club	0	11-25-2010 08:21 PM
[NMR paper] An NMR study of the interaction between the human copper(I) chaperone and the second An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein. Related Articles An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein. FEBS J. 2005 Feb;272(3):865-71 Authors: Banci L, Bertini I, Ciofi-Baffoni S, Chasapis CT, Hadjiliadis N, Rosato A The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] Interaction between the type-3 copper protein tyrosinase and the substrate analogue p Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR. Related Articles Interaction between the type-3 copper protein tyrosinase and the substrate analogue p-nitrophenol studied by NMR. J Am Chem Soc. 2005 Jan 19;127(2):567-75 Authors: Tepper AW, Bubacco L, Canters GW The interaction of the monooxygenating type-3 copper enzyme Tyrosinase (Ty) from Streptomyces antibioticus with its inhibitor p-nitrophenol (pnp) was studied by paramagnetic NMR methods. The pnp binds to oxidized Ty...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR. Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR. Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR. Biochemistry. 2004 Nov 2;43(43):13775-86 Authors: Bann JG, Frieden C The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...	nmrlearner	Journal club	0	11-24-2010 10:03 PM
[NMR paper] Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy. Related Articles Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy. Biochemistry. 2001 Jun 19;40(24):7069-76 Authors: Worrall JA, Kolczak U, Canters GW, Ubbink M The interaction of yeast iso-1-cytochrome c with its physiological redox partner cytochrome c peroxidase has been investigated using heteronuclear NMR techniques. Chemical shift perturbations for both...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Related Articles NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Biochemistry. 1998 Jun 2;37(22):7929-40 Authors: Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision...	nmrlearner	Journal club	0	11-17-2010 11:06 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