quanta program (Polygen GmbH)
90
Structured Review
Polygen GmbH
quanta program
Quanta Program, supplied by Polygen GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/program+quanta/quanta+program/us09969776-374-14-16
Average 90 stars, based on 1 article reviews
Quanta Program, supplied by Polygen GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/program+quanta/quanta+program/us09969776-374-14-16
Average 90 stars, based on 1 article reviews
quanta program - by Bioz Stars,
2026-09
90/100 stars
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other:Article Title: Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. Article Snippet: The importance of amino acid side-chains in helix stability has been investigated by making a series of mutations at the N-caps, (J-caps and internal positions of the solvent-exposed faces of the two a-helices of harnase.. There is a strong posit’ional and context dependence of the effect of a particular amino acid on stability.. Correlations have been found that provide insight into the physical basis of helix stabilization. Article Title: Bovine thrombin complexed with an uncleavable analog of residues 7-19 of fibrinogen A alpha: geometry of the catalytic triad and interactions of the P1', P2', and P3' substrate residues. Article Snippet: The crystal structure of the noncovalent complex of bovine thrombin and a fibrinogen-AR tridecapeptide substrate analog, G17ψ, in which the scissile bond amide nitrogen of Gly-17f has been replaced by a methylene carbon, has been determined at 2.3 Å resolution with an R factor of 17.1%.. The geometry of the active site indicates that the crystal structure is a close model of the true Michaelis complex.. The three independently determined thrombin/G17ψ complexes in the crystal asymmetric unit reveal novel interactions for the P2′ and P3′ residuessPro-18f and Arg-19f, respectivelyson the carboxylterminal side of the scissile bond and confirm previously observed interactions of the P1 (Arg-16f) through P10 (Asp-7f) positions on the amino-terminal side. Article Title: Société Belge De Biochimie et de Biologie Moleculaire Belgische Vereniging Voor Biochemie en Moleculaire Biologie Article Snippet: A great deal of studies have been devoted to thermophilic enzymes, but very little is known about the structure of enzymes from psychrotrophic bacteria.. The enzymes adapted to low temperatures are characterised by a higher specific activity than their mesophilic counterparts in the range of 0 to 20°C and a greater susceptibility to thermal denaturation.. Both properties were tentatively attributed to a looser and more flexible structure of the protein molecule (HOCHACHKA & SOMERO, 1984). |