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rdf:type
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rdfs:seeAlso
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Description
| - In general, the crystallization of proteins is a very complex process. Experiences of many scientists point out that majority of proteins is difficult to crystallize and even if a protein tends to crystallize relatively easily there are many parameters that must be taken into account. There are multiple reasons that point out the difficulty of protein crystal growth. Apparently, protein molecules are very complex (large, flexible molecules often composed of several subunits), relatively chemically and physically unstable (unfolding, hydration requirements, temperature sensitivity) and they have dynamic properties. If the solution changes, the molecule properties (e.g. conformation, charge and size) will change too. Furthermore, every macromolecule is unique in its physical and chemical properties since every amino acid sequence produces a unique three-dimensional structure having distinctive surface characteristics. Thus, conditions applied for one protein can only marginally apply to others
- In general, the crystallization of proteins is a very complex process. Experiences of many scientists point out that majority of proteins is difficult to crystallize and even if a protein tends to crystallize relatively easily there are many parameters that must be taken into account. There are multiple reasons that point out the difficulty of protein crystal growth. Apparently, protein molecules are very complex (large, flexible molecules often composed of several subunits), relatively chemically and physically unstable (unfolding, hydration requirements, temperature sensitivity) and they have dynamic properties. If the solution changes, the molecule properties (e.g. conformation, charge and size) will change too. Furthermore, every macromolecule is unique in its physical and chemical properties since every amino acid sequence produces a unique three-dimensional structure having distinctive surface characteristics. Thus, conditions applied for one protein can only marginally apply to others (en)
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Title
| - Alternative Crystallization Technique: Cross Influence Procedure (CIP)
- Alternative Crystallization Technique: Cross Influence Procedure (CIP) (en)
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skos:prefLabel
| - Alternative Crystallization Technique: Cross Influence Procedure (CIP)
- Alternative Crystallization Technique: Cross Influence Procedure (CIP) (en)
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skos:notation
| - RIV/60076658:12520/12:43884038!RIV13-MSM-12520___
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http://linked.open...avai/predkladatel
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
| - P(ED2.1.00/01.0024), Z(MSM6007665808)
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/60076658:12520/12:43884038
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - CIP; Procedure; Influence; Cross; Technique; Crystallization; Alternative (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...ontrolniKodProRIV
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http://linked.open...i/riv/mistoVydani
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http://linked.open...vEdiceCisloSvazku
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http://linked.open...i/riv/nazevZdroje
| - Crystallization and Materials Science of Modern Artificial and Natural Crystals
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http://linked.open...in/vavai/riv/obor
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http://linked.open...ichTvurcuVysledku
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http://linked.open...v/pocetStranKnihy
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http://linked.open...cetTvurcuVysledku
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http://linked.open...vavai/riv/projekt
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http://linked.open...UplatneniVysledku
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http://linked.open...iv/tvurceVysledku
| - Kutá-Smatanová, Ivana
- Němčovičová, I.
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http://linked.open...n/vavai/riv/zamer
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number of pages
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http://bibframe.org/vocab/doi
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http://purl.org/ne...btex#hasPublisher
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https://schema.org/isbn
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http://localhost/t...ganizacniJednotka
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is http://linked.open...avai/riv/vysledek
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