Results 11 to 20 of about 12,507,251 (357)

Proteins, proteins everywhere [PDF]

open access: yesScience, 2021
The first protein structures were determined by x-ray crystallography in 1957 by John C. Kendrew and Max F. Perutz. As a bioinorganic chemist, I was delighted that the structures were myoglobin and hemoglobin, both heme proteins with big, beautiful iron atoms.
openaire   +2 more sources

Contextualized Protein-Protein Interactions [PDF]

open access: yesPatterns, 2021
Protein-protein interaction (PPI) databases are an important bioinformatics resource, yet existing literature-curated databases usually represent cell-type-agnostic interactions, which is at variance with our understanding that protein dynamics are context specific and highly dependent on their environment.
Anthony Federico, Stefano Monti
openaire   +3 more sources

Protein [PDF]

open access: yesAdvances in Nutrition, 2011
Proteins are polymers of amino acids linked via α-peptide bonds. They can be represented as primary, secondary, tertiary, and even quaternary structures, but from a nutritional viewpoint only the primary (amino acid) sequence is of interest. Similarly, although there are many compounds in the body that can be chemically defined as amino acids, we are ...
Malcolm, Watford, Guoyao, Wu
openaire   +4 more sources

Volatile Compounds, Fatty Acids Constituents, and Antimicrobial Activity of Cultured Spirulina (Arthrospira fusiformis) Isolated from Lake Mariout in Egypt

open access: yesThe Scientific World Journal, 2023
In this study, Arthrospira fusiformis previously isolated from Lake Mariout (Alexandria, Egypt) was cultivated in the laboratory using a medium for pharmaceutical grade Arthrospira, named as Amara and Steinbüchel medium. Hot water extract of the Egyptian
Gamal M. Hamad   +3 more
doaj   +1 more source

Directed evolution converts subtilisin E into a functional equivalent of thermitase [PDF]

open access: yes, 1999
We used directed evolution to convert Bacillus subtilis subtilisin E into an enzyme functionally equivalent to its thermophilic homolog thermitase from Thermoactinomyces vulgaris.
Arnold, Frances H., Zhao, Huimin
core   +2 more sources

Application of fourier transform and proteochemometrics principles to protein engineering

open access: yesBMC Bioinformatics, 2018
Background Connecting the dots between the protein sequence and its function is of fundamental interest for protein engineers. In-silico methods are useful in this quest especially when structural information is not available.
Frédéric Cadet   +6 more
doaj   +1 more source

Minimum energy configurations of the 2-dimensional HP-model of proteins by self-organizing networks [PDF]

open access: yes, 2002
We use self-organizing maps (SOM) as an efficient tool to find the minimum energy configurations of the 2-dimensional HP-models of proteins. The usage of the SOM for the protein folding problem is similar to that for the Traveling Salesman Problem.
Erman, Burak   +2 more
core   +1 more source

Influenza Evolution and H3N2 Vaccine Effectiveness, with Application to the 2014/2015 Season [PDF]

open access: yes, 2016
Influenza A is a serious disease that causes significant morbidity and mortality, and vaccines against the seasonal influenza disease are of variable effectiveness.
Deem, Michael W., Li, Xi
core   +2 more sources

Bacteriophage Protein–Protein Interactions [PDF]

open access: yes, 2012
Bacteriophages T7, λ, P22, and P2/P4 (from Escherichia coli), as well as ϕ29 (from Bacillus subtilis), are among the best-studied bacterial viruses. This chapter summarizes published protein interaction data of intraviral protein interactions, as well as known phage-host protein interactions of these phages retrieved from the literature. We also review
Häuser, R.   +8 more
openaire   +4 more sources

Multiple structural alignment for distantly related all b structures using TOPS pattern discovery and simulated annealing [PDF]

open access: yes, 2003
Topsalign is a method that will structurally align diverse protein structures, for example, structural alignment of protein superfolds. All proteins within a superfold share the same fold but often have very low sequence identity and different biological
Gilbert, D, Westhead, DR, Williams, A
core   +1 more source

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