Gary Keith Ackers | |
---|---|
Born | 1939 |
Died | 2011 |
Nationality | American |
Known for | Agarose gel chromatography |
Scientific career | |
Fields | Thermodynamic linkage analysis of biological macromolecules, cooperative O2 binding to hemoglobin |
Institutions | Washington University in St. Louis |
Gary Keith Ackers (1939 - 2011) [1] was Emeritus Professor of Biochemistry and Molecular Biophysics of Washington University in St. Louis, Missouri.
His research focused on thermodynamic linkage analysis of biological macromolecules, addressing the molecular mechanism of cooperative O2 binding to human hemoglobin since the early 1970s. He was a Fellow of the Biophysical Society and one of the founders of the annual Gibbs Conference. [2]
Professor Ackers invented agarose gel chromatography when he was a teenager. He went on the develop analytical gel chromatography methods for determinations of many important characteristics of water-soluble proteins; diffusion coefficient, molecular size, [3] [4] thermodynamics of protein-protein interactions including important changes due to single amino acid substitutions. [5]
Heme, or haem, is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver.
Irwin Allan Rose was an American biologist. Along with Aaron Ciechanover and Avram Hershko, he was awarded the 2004 Nobel Prize in Chemistry for the discovery of ubiquitin-mediated protein degradation.
Peptide mass fingerprinting (PMF), also known as protein fingerprinting, is an analytical technique for protein identification in which the unknown protein of interest is first cleaved into smaller peptides, whose absolute masses can be accurately measured with a mass spectrometer such as MALDI-TOF or ESI-TOF. The method was developed in 1993 by several groups independently. The peptide masses are compared to either a database containing known protein sequences or even the genome. This is achieved by using computer programs that translate the known genome of the organism into proteins, then theoretically cut the proteins into peptides, and calculate the absolute masses of the peptides from each protein. They then compare the masses of the peptides of the unknown protein to the theoretical peptide masses of each protein encoded in the genome. The results are statistically analyzed to find the best match.
Vernon Martin Ingram, was a German–American professor of biology at the Massachusetts Institute of Technology.
Bone sialoprotein (BSP) is a component of mineralized tissues such as bone, dentin, cementum and calcified cartilage. BSP is a significant component of the bone extracellular matrix and has been suggested to constitute approximately 8% of all non-collagenous proteins found in bone and cementum. BSP, a SIBLING protein, was originally isolated from bovine cortical bone as a 23-kDa glycopeptide with high sialic acid content.
Protein L was first isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind immunoglobulins through L chain interaction, from which the name was suggested. It consists of 719 amino acid residues. The molecular weight of protein L purified from the cell walls of Peptostreptoccus magnus was first estimated as 95kD by SDS-PAGE in the presence of reducing agent 2-mercaptoethanol, while the molecular weight was determined to 76kD by gel chromatography in the presence of 6 M guanidine HCl. Protein L does not contain any interchain disulfide loops, nor does it consist of disulfide-linked subunits. It is an acidic molecule with a pI of 4.0. Unlike protein A and protein G, which bind to the Fc region of immunoglobulins (antibodies), protein L binds antibodies through light chain interactions. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to protein L.
In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction
Apolipoprotein A-IV is plasma protein that is the product of the human gene APOA4.
Phosphoglycerate kinase 1 is an enzyme that in humans is encoded by the PGK1 gene.
Leukotriene-A4 hydrolase is an enzyme that catalyzes the reaction which converts Leukotriene A4 to Leukotriene B4. It is a bifunctional zinc enzyme with different amino acids attached to it to aid in the catalysis of the reaction. It also acts as an aminopeptidase. Leukotriene-A4 hydrolase is a cytosolic protein and is found in almost all mammalian cells, tissues and organelles that have been examined.
Calcium/calmodulin-dependent protein kinase type II gamma chain is an enzyme that in humans is encoded by the CAMK2G gene.
Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.
Glycoprotein Ib (platelet), beta polypeptide (GP1BB) also known as CD42c, is a protein that in humans is encoded by the GP1BB gene.
Glycophorin B (MNS blood group) (gene designation GYPB) also known as sialoglycoprotein delta and SS-active sialoglycoprotein is a protein which in humans is encoded by the GYPB gene. GYPB has also recently been designated CD235b (cluster of differentiation 235b).
Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.
Bile acid-CoA:amino acid N-acyltransferase is an enzyme that in humans is encoded by the BAAT gene.
General transcription factor IIF subunit 2 is a protein that in humans is encoded by the GTF2F2 gene.
Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins. When consecutively measuring amino acids of a protein, changes in value indicate attraction of specific protein regions towards the hydrophobic region inside lipid bilayer.
Synapsin I, is the collective name for Synapsin Ia and Synapsin Ib, two nearly identical phosphoproteins that in humans are encoded by the SYN1 gene. In its phosphorylated form, Synapsin I may also be referred to as phosphosynaspin I. Synapsin I is the first of the proteins in the synapsin family of phosphoproteins in the synaptic vesicles present in the central and peripheral nervous systems. Synapsin Ia and Ib are close in length and almost the same in make up, however, Synapsin Ib stops short of the last segment of the C-terminal in the amino acid sequence found in Synapsin Ia.
Arnold Martin Katz was an American medical doctor, professor of cardiology, medical researcher, and author of medical textbooks and research articles.
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