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 05-31-2020, 03:53 PM
nmrlearner's Avatar
Senior Member
 
Join Date: Jan 2005
Posts: 20,215
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 NMR Spectroscopic Studies Reveal the Critical Role of Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.

NMR Spectroscopic Studies Reveal the Critical Role of Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.

Related Articles NMR Spectroscopic Studies Reveal the Critical Role of Isopeptide Bond in Forming the Otherwise Unstable SpyTag-SpyCatcher Mutant Complexes.

Biochemistry. 2020 May 29;:

Authors: Zhang N, Liu J, Liu Y, Wu W, Fang J, Da XD, Wang S, Zhang WB

Abstract
The interplay between protein folding and chemical reaction has been an intriguing subject. In this contribution, we report the study of SpyTag and SpyCatcher reactive mutants using combined techniques of SDS-PAGE, LC-MS, circular dichroism, and NMR spectroscopy. It was found that the wild-type SpyCatcher is well-folded in solution and docks with SpyTag to form an intermediate that promotes isopeptide formation. By contrast, the double mutant SpyCatcherVA is disordered in solution, yet remains reactive toward SpyTag, forming a well-folded covalent complex. Control experiments using the catalytically inactive mutants further reveal the critical role of the isopeptide bond in stabilizing the otherwise loose SpyTag-SpyCatcherVA complex, amplifying the effect of minute sequence disparity. We believe that the synergy between protein folding and isopeptide bonding is an effective way to enhance protein stability and engineer protein-protein interactions.


PMID: 32469203 [PubMed - as supplied by publisher]



More...
Reply With Quote


Did you find this post helpful? Yes | No

Reply
Similar Threads
Thread Thread Starter Forum Replies Last Post
[NMR paper] Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction.
Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction. Biophysical studies and NMR structure of YAP2 WW domain - LATS1 PPxY motif complexes reveal the basis of their interaction. Oncotarget. 2018 Jan 30;9(8):8068-8080 Authors: Verma A, Jing-Song F, Finch-Edmondson ML, Velazquez-Campoy A, Balasegaran S, Sudol M, Sivaraman J Abstract YES-associated protein (YAP) is a major effector protein of the Hippo tumor suppressor pathway, and is phosphorylated by the...
nmrlearner Journal club 0 03-01-2018 09:20 PM
A non-uniform sampling approach enables studies of dilute and unstable proteins
A non-uniform sampling approach enables studies of dilute and unstable proteins Abstract NMR spectroscopy is a powerful method in structural and functional analysis of macromolecules and has become particularly prevalent in studies of protein structure, function and dynamics. Unique to NMR spectroscopy is the relatively low constraints on sample preparation and the high level of control of sample conditions. Proteins can be studied in a wide range of buffer conditions, e.g. different pHs and variable temperatures, allowing studies of proteins under...
nmrlearner Journal club 0 02-11-2017 12:49 PM
[NMR paper] Quantitative Analysis of STD-NMR Spectra of Reversibly Forming Ligand-Receptor Complexes.
Quantitative Analysis of STD-NMR Spectra of Reversibly Forming Ligand-Receptor Complexes. Related Articles Quantitative Analysis of STD-NMR Spectra of Reversibly Forming Ligand-Receptor Complexes. Top Curr Chem. 2008;273:15-54 Authors: Krishna NR, Jayalakshmi V Abstract We describe our work on the quantitative analysis of STD-NMR spectra of reversibly forming ligand-receptorcomplexes. This analysis is based on the theory of complete relaxation and conformational exchange matrixanalysis of saturation transfer (CORCEMA-ST) effects. As part...
nmrlearner Journal club 0 04-24-2013 09:48 PM
NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond.
NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond. NMR spectroscopic and theoretical analysis of a spontaneously formed Lys-Asp isopeptide bond. Angew Chem Int Ed Engl. 2010 Nov 2;49(45):8421-5 Authors: Hagan RM, Björnsson R, McMahon SA, Schomburg B, Braithwaite V, Bühl M, Naismith JH, Schwarz-Linek U
nmrlearner Journal club 0 02-15-2011 07:17 PM
[NMR paper] The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studie
The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR. Related Articles The role of disulfide bond in the amyloidogenic state of beta(2)-microglobulin studied by heteronuclear NMR. Protein Sci. 2002 Sep;11(9):2218-29 Authors: Katou H, Kanno T, Hoshino M, Hagihara Y, Tanaka H, Kawai T, Hasegawa K, Naiki H, Goto Y beta(2)-Microglobulin (beta2-m) is a major component of dialysis-related amyloid fibrils. Although recombinant beta2-m forms needle-like fibrils by in vitro extension reaction at pH...
nmrlearner Journal club 0 11-24-2010 08:58 PM
[NMR paper] Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interact
Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Related Articles Real-time and equilibrium (19)F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. Proc Natl Acad Sci U S A. 2002 Jan 22;99(2):709-14 Authors: Bann JG, Pinkner J, Hultgren SJ, Frieden C PapD is a periplasmic chaperone essential for P pilus formation in pyelonephritic strains of E. coli. It is composed of two domains, each of which contains a tryptophan...
nmrlearner Journal club 0 11-24-2010 08:49 PM
[NMR paper] NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal g
NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state. Biochemistry. 1997 Mar 25;36(12):3448-57 Authors: Evenäs J, Thulin E, Malmendal A, Forsén S, Carlström G In the present investigation, the Ca2+...
nmrlearner Journal club 0 08-22-2010 03:31 PM
[NMR paper] NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal g
NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR studies of the E140Q mutant of the carboxy-terminal domain of calmodulin reveal global conformational exchange in the Ca2+-saturated state. Biochemistry. 1997 Mar 25;36(12):3448-57 Authors: Evenäs J, Thulin E, Malmendal A, Forsén S, Carlström G In the present investigation, the Ca2+...
nmrlearner Journal club 0 08-22-2010 03:03 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 - 2020, 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 05:32 PM.


Map