NDLI: A paramagnetic probe to localize residues next to carboxylates on protein surfaces

Please wait, while we are loading the content...

Mechanistic studies of the astacin-like Serratia metalloendopeptidase serralysin: highly active (>2000%) Co(II) and Cu(II) derivatives for further corroboration of a "metallotriad" mechanism

A distinct Cu4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain

A paramagnetic probe to localize residues next to carboxylates on protein surfaces

Molecular characterization of Bacillus pasteurii UreE, a metal-binding chaperone for the assembly of the urease active site

Density functional calculation of pK a values and redox potentials in the bovine Rieske iron-sulfur protein

Hard X-ray microprobe studies of chromium(VI)-treated V79 Chinese hamster lung cells: intracellular mapping of the biotransformation products of a chromium carcinogen

The journey from curiosity to function: the mosaic of superoxide reductase is revealed

Superoxide reductase: fact or fiction?

The mechanism(s) of superoxide reduction by superoxide reductases in vitro and in vivo

What biological purpose is served by superoxide reductase?

What is the ultimate fate of superoxide anion in vivo?

Superoxide scavenging by neelaredoxin: dismutation and reduction activities in anaerobes

Erratum to In vitro study of the insulin-mimetic behaviour of vanadium(IV, V) coordination compounds

JBIC Journal of Biological Inorganic Chemistry : Volume 7, Issue 4-5, April 2002

JBIC Journal of Biological Inorganic Chemistry : Volume 7, Issue 3, March 2002

JBIC Journal of Biological Inorganic Chemistry : Volume 7, Issue 1-2, January 2002

JBIC Journal of Biological Inorganic Chemistry : Volume 6

JBIC Journal of Biological Inorganic Chemistry : Volume 5

JBIC Journal of Biological Inorganic Chemistry : Volume 4

JBIC Journal of Biological Inorganic Chemistry : Volume 3

JBIC Journal of Biological Inorganic Chemistry : Volume 2

A paramagnetic probe to localize residues next to carboxylates on protein surfaces

Content Provider	Springer Nature Link
Author	Aime, Silvio D'Amelio, Nicola Fragai, Marco Lee, Yong Min Luchinat, Claudio Terre, Enzo Valensin, Gianni
Copyright Year	2002
Abstract	It is shown that the paramagnetic properties of lanthanides can be exploited to obtain information on specific parts of a protein surface. Owing to the high affinity of coordinatively unsaturated lanthanide complexes for oxygen donors, carboxylate groups can be used as preferential targets for the interaction. The DO3A ligand is particularly useful in these studies, as it coordinates lanthanides in a heptadentate fashion, leaving two sites available for exogenous donors. A solution of a 15N-labeled sample protein, calbindin D9k (75 residues), was titrated with up to 200% of Gd(III)-DO3A complex, and an inversion recovery 15N-1H HSQC experiment was used to measure the paramagnetic contributions to the longitudinal relaxation rates of the amide protons. Relaxation data were used as distance constraints to estimate the number of interacting complexes and the occupancies of their binding sites. Four preferential interaction sites on the protein surface are found. Inspection of the various carboxylate side chains on the surface of the protein indicates that Gd(III)-DO3A interacts preferentially with carboxylate-rich regions, rather than with isolated carboxylates, suggesting the possibility of chelation of one Gd(III)-DO3A molecule by two carboxylate groups. Gd(III)-DO3A is thus a valuable semi-selective probe for clusters of negative charges on the protein surface.
Starting Page	617
Ending Page	622
Page Count	6
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	7
Issue Number	6
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2002-02-14
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Cu(II)-Based Paramagnetic Probe to Study RNA–Protein Interactions by NMR

Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein

An NMR structural study of nickel-substituted rubredoxin

Desulfoferrodoxin: a modular protein

Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study

Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR

Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins

A decadentate Gd(III)-coordinating paramagnetic cosolvent for protein relaxation enhancement measurement

The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues

A paramagnetic probe to localize residues next to carboxylates on protein surfaces

Similar Documents

Cu(II)-Based Paramagnetic Probe to Study RNA–Protein Interactions by NMR

Desulforubrerythrin from Campylobacter jejuni, a novel multidomain protein

An NMR structural study of nickel-substituted rubredoxin

Desulfoferrodoxin: a modular protein

Interaction between dimer interface residues of native and mutated SOD1 protein: a theoretical study

Cobalt-based paramagnetic probe to study RNA-protein interactions by NMR

Obtaining ligand geometries from paramagnetic shifts in low-spin haem proteins

A decadentate Gd(III)-coordinating paramagnetic cosolvent for protein relaxation enhancement measurement

The dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase from Haemophilus influenzae contains two active-site histidine residues

A paramagnetic probe to localize residues next to carboxylates on protein surfaces