[ASAP] Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design

		BioNMR > Educational resources > Journal club
[ASAP] Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design

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

03-05-2022, 01:44 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

[ASAP] Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design

[ASAP] Efficient Exploration of Sequence Space by Sequence-Guided Protein Engineering and Design

Biochemistry
DOI: 10.1021/acs.biochem.1c00757

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[ASAP] Partial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations Partial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00309/20210713/images/medium/bi1c00309_0007.gif Biochemistry DOI: 10.1021/acs.biochem.1c00309 http://feeds.feedburner.com/~r/acs/bichaw/~4/J5d4_89szC4 More...	nmrlearner	Journal club	0	07-14-2021 09:40 AM
[ASAP] Protein Engineering in the Design of Protein–Protein Interactions: SARS-CoV-2 Inhibitors as a Test Case Protein Engineering in the Design of Protein–Protein Interactions: SARS-CoV-2 Inhibitors as a Test Case https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00356/20210701/images/medium/bi1c00356_0003.gif Biochemistry DOI: 10.1021/acs.biochem.1c00356 http://feeds.feedburner.com/~r/acs/bichaw/~4/I1umUsCPml8 More...	nmrlearner	Journal club	0	07-03-2021 08:12 PM
[ASAP] Protein Sequence Selection Method That Enables Full Consensus Design of Artificial l-Threonine 3-Dehydrogenases with Unique Enzymatic Properties Protein Sequence Selection Method That Enables Full Consensus Design of Artificial l-Threonine 3-Dehydrogenases with Unique Enzymatic Properties https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00570/20200925/images/medium/bi0c00570_0005.gif Biochemistry DOI: 10.1021/acs.biochem.0c00570 http://feeds.feedburner.com/~r/acs/bichaw/~4/fsYaXqh1J1g More...	nmrlearner	Journal club	0	09-28-2020 09:16 PM
[ASAP] Engineering of a Brighter Variant of the FusionRed Fluorescent Protein Using Lifetime Flow Cytometry and Structure-Guided Mutations Engineering of a Brighter Variant of the FusionRed Fluorescent Protein Using Lifetime Flow Cytometry and Structure-Guided Mutations https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00484/20200924/images/medium/bi0c00484_0007.gif Biochemistry DOI: 10.1021/acs.biochem.0c00484 http://feeds.feedburner.com/~r/acs/bichaw/~4/ZWnwIs0C-lk More...	nmrlearner	Journal club	0	09-26-2020 07:23 AM
[ASAP] Guest Sequence Can Influence RNA Encapsulation by an Engineered Cationic Protein Capsid Guest Sequence Can Influence RNA Encapsulation by an Engineered Cationic Protein Capsid https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00077/20200413/images/medium/bi0c00077_0006.gif Biochemistry DOI: 10.1021/acs.biochem.0c00077 http://feeds.feedburner.com/~r/acs/bichaw/~4/aUNIHNbp1mA More...	nmrlearner	Journal club	0	04-20-2020 05:10 PM
A reduced dimensionality NMR pulse sequence and an efficient protocol for unambiguous assignment in intrinsically disordered proteins A reduced dimensionality NMR pulse sequence and an efficient protocol for unambiguous assignment in intrinsically disordered proteins Abstract Resonance assignment in intrinsically disordered proteins poses a great challenge because of poor chemical shift dispersion in most of the nuclei that are commonly monitored. Reduced dimensionality (RD) experiments where more than one nuclei are co-evolved simultaneously along one of the time axes of a multi-dimensional NMR experiment help to resolve this problem partially, and one can conceive of different...	nmrlearner	Journal club	0	06-19-2014 10:21 PM
[NMR paper] A reduced dimensionality NMR pulse sequence and an efficient protocol for unambiguous assignment in intrinsically disordered proteins. A reduced dimensionality NMR pulse sequence and an efficient protocol for unambiguous assignment in intrinsically disordered proteins. Related Articles A reduced dimensionality NMR pulse sequence and an efficient protocol for unambiguous assignment in intrinsically disordered proteins. J Biomol NMR. 2014 May 23; Authors: Reddy JG, Hosur RV Abstract Resonance assignment in intrinsically disordered proteins poses a great challenge because of poor chemical shift dispersion in most of the nuclei that are commonly monitored....	nmrlearner	Journal club	0	05-24-2014 04:50 PM
[NMR paper] An efficient NMR approach for obtaining sequence-specific resonance assignments of la An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling. FEBS Lett. 1990 Jun 18;266(1-2):155-8 Authors: Ikura M, Krinks M, Torchia DA, Bax A By simultaneously incorporating in a protein 13C-carbonyl- and...	nmrlearner	Journal club	0	08-21-2010 10:48 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