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, 02:27 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 17,582
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 H-NMR study of temperature-induced structure alteration at the active site of horse h

H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.

Related Articles H-NMR study of temperature-induced structure alteration at the active site of horse heart cytochrome c.

J Biochem. 1996 Jan;119(1):16-22

Authors: Yamamoto Y

The molecular structure of the active site of horse heart met-cyano cytochrome c, as a function of temperature, has been investigated using 1H-NMR. A temperature dependence study of the NMR spectra revealed that one heme methyl proton resonance exhibits anti-Curie behavior, i.e., the hyperfine shift increases with increasing temperature. Analyses of the average heme methyl proton hyperfine shift and the proximal His imidazole proton resonances indicated that the iron-His bonding interaction in this protein is essentially independent of temperature. Since such an anomalous temperature dependence of the heme methyl proton resonance disappears in met-cyano complex of a heme peptide prepared by enzymatic degradation of the protein [Smith, M. and McLendon, G. (1981) J. Am. Chem. Soc. 103, 4912-4921], the anti-Curie behavior observed for the heme methyl proton resonance in met-cyano cytochrome c is attributed to a rotational displacement of the heme about the iron-His bond relative to the protein moiety due to a temperature-dependent conformational alteration of the heme-protein linkage. Such rotational mobility of heme at the active site of a protein may be responsible for the anomalous temperature dependence of heme methyl proton hyperfine shifts reported for many c-type ferri cytochromes.

PMID: 8907170 [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
Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A 1H NMR Study
Influence of Substrate Modification and C-Terminal Truncation on the Active Site Structure of Substrate-Bound Heme Oxygenase from Neisseriae meningitidis. A 1H NMR Study http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi200978g/aop/images/medium/bi-2011-00978g_0009.gif Biochemistry DOI: 10.1021/bi200978g http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA http://feeds.feedburner.com/~r/acs/bichaw/~4/BYT7Ijd6pDI More...
nmrlearner Journal club 0 09-22-2011 05:37 AM
[NMR paper] Solution 1H NMR study of the active site molecular structure and magnetic properties
Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin. Related Articles Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin. Biochim Biophys Acta. 2004 Sep 1;1701(1-2):75-87 Authors: Tran AT, Kolczak U, La Mar GN The solution molecular structure and the electronic and magnetic properties of the heme...
nmrlearner Journal club 0 11-24-2010 10:01 PM
[NMR paper] Two-dimensional NMR study of the heme active site structure of chloroperoxidase.
Two-dimensional NMR study of the heme active site structure of chloroperoxidase. Related Articles Two-dimensional NMR study of the heme active site structure of chloroperoxidase. J Biol Chem. 2003 Mar 7;278(10):7765-74 Authors: Wang X, Tachikawa H, Yi X, Manoj KM, Hager LP The heme active site structure of chloroperoxidase (CPO), a glycoprotein that displays versatile catalytic activities isolated from the marine mold Caldariomyces fumago, has been characterized by two-dimensional NMR spectroscopic studies. All hyperfine shifted resonances...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation o
Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR. Related Articles Alteration of conformation and dynamics of bacteriorhodopsin induced by protonation of Asp 85 and deprotonation of Schiff base as studied by 13C NMR. Biochemistry. 2000 Nov 28;39(47):14472-80 Authors: Kawase Y, Tanio M, Kira A, Yamaguchi S, Tuzi S, Naito A, Kataoka M, Lanyi JK, Needleman R, Sait˘ H According to previous X-ray diffraction studies, the D85N mutant of...
nmrlearner Journal club 0 11-19-2010 08:29 PM
[NMR paper] 13C magic angle spinning NMR study of the light-induced and temperature-dependent cha
13C magic angle spinning NMR study of the light-induced and temperature-dependent changes in Rhodobacter sphaeroides R26 reaction centers enriched in tyrosine. Related Articles 13C magic angle spinning NMR study of the light-induced and temperature-dependent changes in Rhodobacter sphaeroides R26 reaction centers enriched in tyrosine. Biochemistry. 1992 Nov 17;31(45):11038-49 Authors: Fischer MR, de Groot HJ, Raap J, Winkel C, Hoff AJ, Lugtenburg J Solid-state 13C magic angle spinning (MAS) NMR has been used to investigate...
nmrlearner Journal club 0 08-21-2010 11:45 PM
[NMR paper] Rotational resonance NMR study of the active site structure in bacteriorhodopsin: con
Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage. Related Articles Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage. Biochemistry. 1992 Sep 1;31(34):7931-8 Authors: Thompson LK, McDermott AE, Raap J, van der Wielen CM, Lugtenburg J, Herzfeld J, Griffin RG Rotational resonance, a new solid-state NMR technique for determining internuclear distances, is used to measure a distance in the active site of...
nmrlearner Journal club 0 08-21-2010 11:45 PM
[NMR paper] 1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse,
1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse, and sperm whale deoxy myoglobins. Related Articles 1H-NMR comparative study of the active site in shark (Galeorhinus japonicus), horse, and sperm whale deoxy myoglobins. J Biochem. 1992 Sep;112(3):414-20 Authors: Yamamoto Y, Iwafune K, Ch├╗j├┤ R, Inoue Y, Imai K, Suzuki T 1H-NMR spectra of deoxy myoglobins (Mbs) from shark (Galeorhinus japonicus), horse, and sperm whale have been studied to gain insights into their active site structure. It has been...
nmrlearner Journal club 0 08-21-2010 11:45 PM
[NMR paper] A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus me
A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin. 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 A 1H-NMR study of electronic structure of the active site of Galeorhinus japonicus metmyoglobin. Eur J Biochem. 1990 Aug 28;192(1):225-9 Authors: Yamamoto Y, Osawa A, Inoue Y, Ch├╗j├┤ R, Suzuki T The ferric high-spin form of the myoglobin from the shark Galeorhinus japonicus, which...
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 05:38 AM.


Map