Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease - pnas.org

		BioNMR > NMR community > Online News
Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease - pnas.org

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

04-23-2022, 11:15 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

Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease - pnas.org

Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease - pnas.org

Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease pnas.org Read here

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein - pnas.org Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein - pnas.org Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein pnas.org Read here	nmrlearner	Online News	0	03-26-2022 07:08 PM
Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein - pnas.org Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein - pnas.org Dissecting the role of interprotomer cooperativity in the activation of oligomeric high-temperature requirement A2 protein pnas.org Read here	nmrlearner	Online News	0	08-26-2021 10:50 PM
Structural basis of client specificity in mitochondrial membrane-protein chaperones - Science Advances Structural basis of client specificity in mitochondrial membrane-protein chaperones - Science Advances Structural basis of client specificity in mitochondrial membrane-protein chaperones Science Advances Read here	nmrlearner	Online News	0	01-03-2021 01:46 PM
Structural basis of client specificity in mitochondrial membrane-protein chaperones - Science Advances Structural basis of client specificity in mitochondrial membrane-protein chaperones - Science Advances Structural basis of client specificity in mitochondrial membrane-protein chaperones Science Advances Read here	nmrlearner	Online News	0	12-29-2020 04:50 AM
[NMR paper] Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study. Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study. Related Articles Mechanistic basis of substrate-O2 coupling within a chitin-active lytic polysaccharide monooxygenase: An integrated NMR/EPR study. Proc Natl Acad Sci U S A. 2020 Jul 28;: Authors: Courtade G, Ciano L, Paradisi A, Lindley PJ, Forsberg Z, Sørlie M, Wimmer R, Davies GJ, Eijsink VGH, Walton PH, Aachmann FL Abstract Lytic polysaccharide monooxygenases (LPMOs) have a unique ability to...	nmrlearner	Journal club	0	07-30-2020 05:28 PM
[NMR paper] Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR. Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--www.ncbi.nlm.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR. Proc...	nmrlearner	Journal club	0	06-27-2018 01:51 AM
[NMR paper] High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release. High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release. http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--academic.oup.com-images-oup_pubmed.png Related Articles High-resolution crystal structures and STD NMR mapping of human ABO(H) blood group glycosyltransferases in complex with trisaccharide reaction products suggest a molecular basis for product release. Glycobiology. 2017 Oct 01;27(10):966-977...	nmrlearner	Journal club	0	05-24-2018 01:05 PM
[NMR paper] NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity. NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity. Related Articles NMR Structure of the APOBEC3B Catalytic Domain: Structural Basis for Substrate Binding and DNA Deaminase Activity. Biochemistry. 2016 May 10; Authors: Byeon IL, Byeon CH, Wu T, Mitra M, Singer D, Levin JG, Gronenborn AM Abstract Human APOBEC3B (A3B) is a member of the APOBEC3 (A3) family of cytidine deaminases, which function as DNA mutators and restrict viral pathogens and endogenous...	nmrlearner	Journal club	0	05-11-2016 08:04 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