Results 251 to 260 of about 7,456,122 (302)

On the “tertiary” structure of chromosomes

Mutation Research, 1970
Abstract Although we know chromosomes consist of both nucleic acids and protein, we are still unsure about the actual organization of these components in chromosomes as they are seen in mitosis. Radiation studies in which chromosomes aberrations are induced at various stages of the cell cycle have indicated that chromosomes react as though they were ...
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On the tertiary structure of satellite DNA

Biochimie, 1992
The primary structure of the Citrus ichangensis satellite DNA repeating unit has been estimated. The repeat is 181 bp long and contains four pentanucleotides of adenine residues. Oligomer forms of the stDNA repeating unit were detected by a partial hydrolysis of the C ichangensis stDNA by BspI restriction endonuclease.
T, Beridze, N, Tsirekidze, M A, Roytberg
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Evolution and the Tertiary Structure of Proteins

Annual Review of Biophysics and Bioengineering, 1984
The fact that biological information is stored in the form of DNA has led some molecular biologists and biophysicists to the view that evolutionary history will be most evident in DNA sequences. This view is attractive, for there is a redundancy in the genetic code, and the number of base changes is a sensitive indicator of evolutionary distances ...
M, Bajaj, T, Blundell
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Protein Tertiary Structure Modeling

Current Protocols in Protein Science, 2001
AbstractInsights into the 3D‐structure of a protein have proven useful during experiment design. Experimentally elucidated structures are often not available, but comparative protein modeling provides a viable alternative in many cases. This unit presents comparative protein modeling and how to use the highly sophisticated but easy‐to‐use free software
Guex, N., Schwede, T., Peitsch, M. C.
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Calculation of protein tertiary structure

Journal of Molecular Biology, 1976
Abstract We describe a method for calculating the tertiary structure of proteins given their amino acid sequence. The algorithm involves locally minimizing an energylike expression as a function of the Cartesian co-ordinates of the C β of all residues.
I D, Kuntz, G M, Crippen, P A, Kollman, D, Kimelman   +3 more
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Quaternary and tertiary structure of haemerythrin

Nature, 1975
THE oligomeric protein haemerythrin is an oxygen-transport pigment found in erythrocytes of the coelomic fluid of certain invertebrates. It usually occurs as an octamer of molecular weight 108,000, in which each sub-unit contains two Fe atoms and reversibly binds one O2 molecule1.
K B, Ward, W A, Hendrickson, G L, Klippenstein   +2 more
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Serpin tertiary structure transformation

Journal of Molecular Biology, 1991
Previous crystallographic analyses have demonstrated that proteolytic cleavage of the serpins can result in a dramatic transformation of their tertiary structure. Some 16 residues on the amino terminal side of the cleavage site are inserted into a large beta-sheet to become a central strand, separating the two cleaved residues by about 70 A.
P, Stein, C, Chothia
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A model for the tertiary structure of tRNA

Biochemical and Biophysical Research Communications, 1973
Abstract A model for tRNA is described which has as its basic structural mode a four stranded RNA helix, formed by pairing two stems respectively from the four ubiquitous arms of the clover-leaf secondary structure. The relation of the model to biochemical and crystallographic data on tRNA is considered.
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Unfolding of tertiary structures of proteins

International Journal of Peptide and Protein Research, 1984
The unfolding pathway of lysozyme was investigated by carrying out the computer simulation. Taking into account the simultaneous change of both the dihedral angles ø and of a residue, we explore the detailed features of the conformational energy profiles. The triangle distance map shows that the lysozyme molecule is divided into three domains, 1–40, 41–
H, Wakana, H, Yokomizo, H, Wako, Y, Isogai, K, Kosuge, N, Saito   +5 more
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Secondary and Tertiary Structure of Apolipoproteins

1988
The advent of these and other high-powered techniques for the detailed study of apoLP organization will allow us to obtain a high resolution picture of apoLP conformation both in solution and on native lipoprotein particles.
M T, Walsh, J A, Hamilton, D, Atkinson, D M, Small   +3 more
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