NDLI: Proton longitudinal relaxation investigation of histidyl residues in human normal adult hemoglobin.

Content Provider	PubMed Central
Author	Ho, C. Russu, I. M.
Abstract	The longitudinal relaxation of the C2 protons of surface histidyl residues as well as other aromatic protons of human normal adult deoxyhemoglobin investigated at 360 MHz is discussed in terms of the theory proposed by Kalk and Berendsen for the proton longitudinal relaxation in proteins (Kalk, A., and H.J.C. Berendsen. 1976. J. Magn. Reson. 24:343-366). The role of the four paramagnetic iron atoms of deoxyhemoglobin as fast-relaxing sinks for the overall proton longitudinal relaxation is evaluated according to the model proposed by Bloembergen for the relaxation of nuclei in crystals containing paramagnetic centers (Bloembergen, N. 1949. Physica. 15:386-426). The results suggest that the effectiveness of the paramagnetic iron atoms of deoxyhemoglobin for the overall proton longitudinal relaxation is reduced as a result of slower spin diffusion and wide distribution of methyl groups within the hemoglobin molecule. Thus, deoxyhemoglobin provides a good model for investigating the influence of cross relaxation on proton longitudinal relaxation in proteins at the slow motion limit and in the presence of paramagnetic centers. For the C2 protons of surface histidyl residues, we show that the cross relaxation resulting from the interresidue dipolar interaction makes an important contribution to their longitudinal relaxation.
Related Links	http://dx.doi.org/10.1016/s0006-3495(82)84509-8
Ending Page	210
Page Count	8
Starting Page	203
File Format	PDF
ISSN	00063495
e-ISSN	15420086
Journal	Biophysical Journal
Issue Number	2
Volume Number	39
Language	English
Publisher Date	1982-08-01
Access Restriction	Open
Subject Keyword	Biophysics Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Biophysics

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

Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions.

Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions.

A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.

Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography

Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin *

Rotational and translational water diffusion in the hemoglobin hydration shell: dielectric and proton nuclear relaxation measurements.

ON THE DISSOCIATION OF NORMAL ADULT HUMAN HEMOGLOBIN

Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.

1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells.

Proton longitudinal relaxation investigation of histidyl residues in human normal adult hemoglobin.

Similar Documents

Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions.

Proton longitudinal relaxation investigation of histidyl residues of normal human adult and sickle deoxyhemoglobin: evidence for the existence of pregelation aggregates in sickle deoxyhemoglobin solutions.

A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.

Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography

Proton nuclear magnetic resonance investigation of structural changes associated with cooperative oxygenation of human adult hemoglobin *

Rotational and translational water diffusion in the hemoglobin hydration shell: dielectric and proton nuclear relaxation measurements.

ON THE DISSOCIATION OF NORMAL ADULT HUMAN HEMOGLOBIN

Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.

1H-NMR investigation of the oxygenation of hemoglobin in intact human red blood cells.

Proton longitudinal relaxation investigation of histidyl residues in human normal adult hemoglobin.