Results 251 to 260 of about 166,818 (301)

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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Probing Protein Tertiary Structure with Amidination

Analytical Chemistry, 2005
A chemical derivatization method, amidination, that has recently been effectively employed in peptide mass spectrometry experiments is used to covalently modify lysines in several standard proteins. Protein and peptide mass spectra identify sites at which the reaction does or does not occur.
Dariusz J, Janecki, Richard L, Beardsley, James P, Reilly   +2 more
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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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Recognition of coarse‐grained protein tertiary structure

Proteins: Structure, Function, and Bioinformatics, 2004
AbstractA model of the protein backbone is considered in which each residue is characterized by the location of its Cα atom and one of a discrete set of conformal (ϕ, ψ) states. We investigate the key differences between a description that offers a locally precise fit to known backbone structures and one that provides a globally accurate fit to protein
LEZON T, BANAVAR J, MARITAN, AMOS
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Computing tertiary structures of proteins

Journal of Protein Chemistry, 1990
Using only data on sequence, a method of computing a low-resolution tertiary structure of a protein is described. The steps are: (a) Estimate the distances of individual residues from the centroid of the molecule, using data on hydrophobicity and additional geometrical constraints. (b) Using these distances, construct a two-valued matrix whose elements,
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Phylogenetics: Tertiary protein structures needed

Nature Ecology & Evolution, 2017
We need to estimate protein tertiary structure, as well as using primary sequences, in order to further our understanding of protein evolution and evolutionary processes in general.
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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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Hydrophobic moments of tertiary protein structures

Proteins: Structure, Function, and Bioinformatics, 2003
AbstractThe helical hydrophobic moment is a measure of the amphiphilicity of a segment of protein secondary structure. Such measure yields information of potential relevance for issues relating to cell surface binding and secondary structure function. The present article describes a global analog of the helical hydrophobic moment.
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Ab initio Tertiary Structure Prediction of Proteins

Journal of Global Optimization, 2003
zbMATH Open Web Interface contents unavailable due to conflicting licenses.
Klepeis, J. L., Floudas, C. A.
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Comparison of homologous tertiary structures of proteins

Journal of Theoretical Biology, 1974
Homology in sequences of proteins which have the same or similar function has been studied as a problem of comparative biochemistry and molecular evolution. It is therefore of interest to examine homology in three-dimensional structures, e.g. whether folding of polypeptides having common residues gives rise to the same tertiary structure or not.
K, Nishikawa, T, Ooi
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