The Application of the Oil Turbine Type of Ultracentrifuge to the Study of the Stability Region of Carbon Monoxide-Hemoglobin

Svedberg, The; Nichols, J. B.

doi:10.1021/ja01410a046

Cited by 66 publications

(16 citation statements)

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“…The dimeric interface is formed by the swapping of a helix folding onto the beta sheet of the other monomer, with an enormous buried surface area resulting in an intimate and very stable dimer. 1 However, the evaluation unit for the regular prediction was the full monomer (including the swapped helix) in all three F I G U R E 3 Performance comparison between CASP13 and CASP12. Five top predictions per target (maximum 1 per group) were selected for each score from CASP12 and CASP13 submissions.…”

Section: Importance Of Quaternary Modelingmentioning

confidence: 99%

“…In their physiological environment, protein chains commonly associate with other chains or copies of themselves to form protein assemblies. This is the so‐called quaternary structure, an intrinsic property of the native state of a protein, known before the first atomic structures were solved . Protein function is linked and often is determined or regulated by the oligomeric structure .…”

Section: Introductionmentioning

confidence: 99%

“…This is the so-called quaternary structure, an intrinsic property of the native state of a protein, known before the first atomic structures were solved. 1 Protein function is linked and often is determined or regulated by the oligomeric structure. [2][3][4] As of March 2019, the average structure in the Protein Data Bank (PDB) 5 is a dimer and approximately half of the PDB is annotated as oligomeric.…”

Section: Introductionmentioning

confidence: 99%

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Assessment of protein assembly prediction in CASP13

et al. 2019

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We present the assembly category assessment in the 13th edition of the CASP community‐wide experiment. For the second time, protein assemblies constitute an independent assessment category. Compared to the last edition we see a clear uptake in participation, more oligomeric targets released, and consistent, albeit modest, improvement of the predictions quality. Looking at the tertiary structure predictions, we observe that ignoring the oligomeric state of the targets hinders modeling success. We also note that some contact prediction groups successfully predicted homomeric interfacial contacts, though it appears that these predictions were not used for assembly modeling. Homology modeling with sizeable human intervention appears to form the basis of the assembly prediction techniques in this round of CASP. Future developments should see more integrated approaches where subunits are modeled in the context of the assemblies they form.

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Section: Importance Of Quaternary Modelingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Assessment of protein assembly prediction in CASP13

et al. 2019

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“…of distilled water was placed in a tall beaker and maintained at 40 irig solution (6.35) was brought to 9.0 by tlie addition uf 3.25 ml. A solution of 0.91 g. of purified hemoglobin in 100 ml.…”

Section: Methodsmentioning

confidence: 99%

The N-Terminal Amino Acid Residues of Normal Adult Human Hemoglobin: A Quantitative Study of Certain Aspects of Sanger's DNP-Method

Rhinesmith¹,

Schroeder²,

Pauling³

1957

J. Am. Chem. Soc.

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A quantitative redetermination of the N-terminal valyl residues of normal adult human hemoglobin by the DNP-method of Sanger has led us to question the validity of results previously reported. Our experimental results indicate that there are 3.6 N-terminal valyl residues per molecule, based on a molecular weight of 66,700 for human hemoglobin. The essential difference between this value and those of other investigators lies in a correction factor for operational, chromatographic and hydrolytic losses (13%) which is appreciably lower than any previously reported value. This low value is justified by a detailed study of losses with DNP-valine and two peptides, DNP-Val-gly and DNP-Val-leu, the latter an important hydrolytic product of human hemoglobin itself. On the basis of these results an integral value for the number of end groups in human hemoglobin can be achieved only by revising the molecular weight, If, on the other hand, the number of N-terminal valyl residues in human hemoglobin is non-integral, it may well indicate that normal adult human hemoglobin contains more than one kind of molecule.

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“…First oil-turbine ultracentrifuge with rotor and cell(Svedberg and Nichols, 1927).For uluacenmfupe: A1, A2. Centrifuge casing F. Oil outlets and oil drains B. Bolts L1.…”

mentioning

confidence: 99%

Svedberg — Discoverer of the protein macromolecules

Rånby

1995

Macromolecular Symposia

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The(odor) Svedberg* (1884‐1971), Uppsala University, was the first professor of physical chemistry in Sweden. He started his research in 1904 as a colloid chemist. He prepared inorganic dispersions by electrical discharge through organic liquids, measured particle size and size distribution of colloids by diffusion and sedimentation rates and invented the ultracentrifuge for convection‐free sedimentation of colloidal particles. In 1924 Svedberg applied the ultracentrifuge for studies of haemoglobin in aqueous solution. Unexpectedly he found that the protein was not a gel of associated small molecules. It sedimented as macromolecules of uniform mass (68 000 dalton), i.e. is monodisperse. In subsequent work Svedberg found that other proteins like ovalbumin (from egg white) and haemocyanins from snails and other invertebrates also are monodisperse or contain a few uniform macromolecular components. After extensive studies of soluble protein molecules from a large number of animals and plants, Svedberg classified the species and could trace the relations for the species from the molecular mass of their protein macromolecules. Studies of soluble polysaccharides from bulbs also showed well defined macromolecules of masses that could be related to the various botanical species. Other native substances like cellulose, other wood polysaccharides and starch were found to be of high molecular mass but polydisperse. Svedberg's research in the 1920's and 1930's gave strong experimental support for Staudinger's macromolecular concept although Svedberg, at the time of his own important discoveries, was not influenced by Staudinger. Svedberg's discovery of the protein macromolecules and their uniform molecular mass initiated the macromolecular research in biochemistry.

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The Application of the Oil Turbine Type of Ultracentrifuge to the Study of the Stability Region of Carbon Monoxide-Hemoglobin

Cited by 66 publications

References 0 publications

Assessment of protein assembly prediction in CASP13

Assessment of protein assembly prediction in CASP13

The N-Terminal Amino Acid Residues of Normal Adult Human Hemoglobin: A Quantitative Study of Certain Aspects of Sanger's DNP-Method

Svedberg — Discoverer of the protein macromolecules

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