Structural significance of the amino terminal residues in human hemoglobin

Thesis/Dissertation · Wed Jan 01 04:00:00 EST 1986

OSTI ID:5348022

Hefta, S A

The amino terminal valine residues on the alpha chains of human hemoglobin are known to be important for the function of the molecule. Allosteric effectors such as protons, chloride ions and metabolic anions such as 2,3-diphosphoglycerate bind or associate with these residues and facilitate the release of oxygen. Carbon dioxide also functions as an effector as it is partly transported from the tissues to the lungs by binding to the amino terminal residues. This research describes the semisynthetic alteration of this region and the hemoglobin analogs produced were analyzed by /sup 13/C NMR.

• Research Organization: Indiana Univ., Bloomington (USA)
• OSTI ID: 5348022
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
CARBON 13
CARBON ISOTOPES
CARBOXYLIC ACIDS
EVEN-ODD NUCLEI
GLOBIN
HEMOGLOBIN
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MOLECULAR STRUCTURE
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PIGMENTS
PORPHYRINS
PROTEINS
RESIDUES
RESONANCE
SPECTRA
STABLE ISOTOPES
VALINE