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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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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.
openaire   +2 more sources

Efficient Approaches for Retrieving Protein Tertiary Structures

IEEE/ACM Transactions on Computational Biology and Bioinformatics, 2012
The 3D conformation of a protein in the space is the main factor which determines its function in living organisms. Due to the huge amount of newly discovered proteins, there is a need for fast and accurate computational methods for retrieving protein structures.
Georgina Mirceva   +3 more
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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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Tertiary Structure of Proteins

2010
In Chapter 4, we gave a brief introduction to proteins. The structures of a very large number of proteins have been determined and it is possible to ask fundamental questions: Given the primary sequence, what is tertiary structure? How does the protein fold into the final structure? This “folding problem” has attracted a great deal of attention, and it
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From Ramachandran Maps to Tertiary Structures of Proteins

The Journal of Physical Chemistry B, 2015
Sequence to structure of proteins is an unsolved problem. A possible coarse grained resolution to this entails specification of all the torsional (Φ, Ψ) angles along the backbone of the polypeptide chain. The Ramachandran map quite elegantly depicts the allowed conformational (Φ, Ψ) space of proteins which is still very large for the purposes of ...
Debarati, DasGupta   +2 more
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Effect of methyl substitution on protein tertiary structure

Journal of Theoretical Biology, 1992
Biological effects caused by the post-translational methylation of certain side chains in proteins has been thought to be due solely to changes in charge, steric relations or hydrophobicity at the site of the methyl group. However, there is increasing evidence that the presence of CH3 can also induce a "global" effect on the protein molecule.
W K, Paik, S, Kim
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Protein denaturation and tertiary structure

Journal of Chemical Education, 1986
Students may dutifully learn the concepts of protein structure, but meaning is often abstracted due to the lack of opportunity for observing the physical entity. To bridge this gap, an inexpensive denaturation experiment is designed to demonstrate the presence of tertiary structure.
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Describing patterns of protein tertiary structure

1985
Publisher Summary This chapter discusses the four major categories of tertiary structure within which subtypes that are more specific described: (1) antiparallel a, (2) parallel α/β, (3) antiparallel β, and (4) small irregular proteins. Within this first major category, the simplest type of structure is the up-and-down helix bundle: an approximate ...
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The MULTICOM Protein Tertiary Structure Prediction System

2013
With the expansion of genomics and proteomics data aided by the rapid progress of next-generation sequencing technologies, computational prediction of protein three-dimensional structure is an essential part of modern structural genomics initiatives. Prediction of protein structure through understanding of the theories behind protein sequence-structure
Jilong, Li   +6 more
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