From 4cbc9a1febf5db4d8463a8be05f1845984c885b1 Mon Sep 17 00:00:00 2001 From: Johan Dahlin Date: Tue, 18 Nov 2025 13:29:40 +0100 Subject: [PATCH] Update --- .gitignore | 2 + .idea/dataSources.xml | 19 + .../shelved.patch | 437 ------------------ ..._Update_at_2025-11-06__19_22__Changes_.xml | 4 - .idea/workspace.xml | 54 ++- content/.obsidian/workspace.json | 2 + content/Biokemi/Proteinseminarie/Frågor.md | 10 +- content/Biokemi/Proteinseminarie/Stödord.md | 18 +- 8 files changed, 86 insertions(+), 460 deletions(-) create mode 100644 .idea/dataSources.xml delete mode 100644 .idea/shelf/Uncommitted_changes_before_Update_at_2025-11-06,_19_22_[Changes]/shelved.patch delete mode 100644 .idea/shelf/Uncommitted_changes_before_Update_at_2025-11-06__19_22__Changes_.xml diff --git a/.gitignore b/.gitignore index 3c3629e..245b599 100644 --- a/.gitignore +++ b/.gitignore @@ -1 +1,3 @@ node_modules +.idea/ +.obsidian/ diff --git a/.idea/dataSources.xml b/.idea/dataSources.xml new file mode 100644 index 0000000..f51e0e6 --- /dev/null +++ b/.idea/dataSources.xml @@ -0,0 +1,19 @@ + + + + + sqlite.xerial + true + org.sqlite.JDBC + jdbc:sqlite:$USER_HOME$/Library/Application Support/Anki2/User 1/collection.anki2 + $ProjectFileDir$ + + + sqlite.xerial + true + org.sqlite.JDBC + jdbc:sqlite:$USER_HOME$/Library/Application Support/Anki2/User 1/collection.media.db2 + $ProjectFileDir$ + + + \ No newline at end of file diff --git a/.idea/shelf/Uncommitted_changes_before_Update_at_2025-11-06,_19_22_[Changes]/shelved.patch b/.idea/shelf/Uncommitted_changes_before_Update_at_2025-11-06,_19_22_[Changes]/shelved.patch deleted file mode 100644 index 6f87dca..0000000 --- a/.idea/shelf/Uncommitted_changes_before_Update_at_2025-11-06,_19_22_[Changes]/shelved.patch +++ /dev/null @@ -1,437 +0,0 @@ -Index: package-lock.json -IDEA additional info: -Subsystem: com.intellij.openapi.diff.impl.patch.BaseRevisionTextPatchEP -<+>{\n \"name\": \"@jackyzha0/quartz\",\n \"version\": \"4.5.2\",\n 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"optional": true, -- "os": [ -- "win32" -- ], -- "peer": true, -- "engines": { -- "node": ">=14.0.0" -- } -- }, - "node_modules/satori": { - "version": "0.18.3", - "resolved": "https://registry.npmjs.org/satori/-/satori-0.18.3.tgz", -Index: content/Biokemi/Från aminosyror till proteiner/Frågeställning I.md -IDEA additional info: -Subsystem: com.intellij.openapi.diff.impl.patch.BaseRevisionTextPatchEP -<+>\nFrågor från första sliden\n• Vad är en aminosyra?\n• Vad menas med stereoisomerer?\n• Vilka egenskaper har de aminosyror som bygger upp proteiner?\n• Hur bildas en peptidbindning och vilka egenskaper har den?\n• Vad innebär primär- och sekundärstruktur hos proteiner?\n• Vad innebär sekundär-, tertiär- och kvartärstruktur hos proteiner?\n\nII:\n• Vad är en proteindomän?\n• Hur sker proteinveckning?\n• Hur stabiliseras ett proteins struktur?\n• Var hittas disulfidbindningar i proteiner?\n• Hur kan ett proteins struktur kopplas till dess funktion?\n• Hur kan felveckning av proteiner orsaka sjukdom?\n#### Vad karaktäriserar en svag bas?\nEtt högt $kP_b$-värde, vilket gör att den tillsammans med sin konjugerande syra fungerar som en buffert +/-1pH av $kP_a \\pm 1$ pH\n#### Hur är en aminosyra uppbyggd?\nDen har ett alfakol som är bundet till fyra grupper:\n- en aminogrupp ($-NH2$ eller $-NH3^-$)\n- en karboxylgrupp ($-COOH$ eller $-COO^-$)\n- en väteatom ($-H$)\n- och en sidogrupp ($-R$) som avgör aminosyrans egenskaper\n#### Vad menas med ett kiralt kol?\nEtt kol som är asymmetriskt med fyra olika funktionella grupper.\n#### Hur skiljs stereoisomerer åt?\nDe har samma kemiska formel men skilja sig i hur det är geometriskt orienterande, finns två sätt att gruppera, antingen prioriteringsordning (CIP-regler) för att bestämma om det går medsols (R) eller motsols (S). L/D som anger hur planpolariserat ljus vrids av molekylen\n#### Vilken stereoisomer av aminosyror används för att bygga upp proteiner?\nInom denna kursen bara L, men det finns enstaka undantag där de använder D.\n#### Vilken aminosyra har ingen stereoisomer och varför?\nGlycin, den ser likadan ut hur man än vrider, det krävs en R-sidokedja som är mer än bara en väteatom för att stereoisomer har en betydelse. Det finns inget kiralt center\n#### Vilken nettoladdning har de flesta aminosyror vid neutralt pH?\nDet har noll-nettoladdning eftersom det är zwitterjoner, aminogruppen är protonerad (+) och kaboxylgruppen är deprotonerad (-).\n#### Vilka aminosyror är alifatiska?\nDe aminosyror som är opolära och icke-aromatiska (utan ringar) är:\n- Glycin\n- Valin\n- Leucin\n- Isoleucin\n- Alinin\n- Metionin\n- Prolin\n#### Vilka egenskaper har alifatiska aminosyror?\nDet är hydrofoba, opolära, saknar ringar, de har bara mättade kolkedjor\n#### Vilka aminosyror är aromatiska?\nFenylalanin\nTryptofan\n#### Vilka egenskaper har aromatiska aminosyror?\nDe är hydrofoba, opolära och absorberar UV-ljus.\n#### I vilken typ av bindningar/interaktioner deltar sidogrupperna hos hydrofoba aminosyror?\nEftersom de mest består av kol och väte är det huvudsakligen van der waals-krafter\n#### Vilka aminosyror är polära?\n- Alkoholer: Serin, Treonin, Tyrosin\n- Tioler: Cystein\n- Amider: Aspargarin, Glutamin\n- Imadazol: Histidin\n#### Vilka egenskaper har polära aminosyror?\nDe är hydrofila, vänder sig mot vattnet/cytoplasman\n#### I vilken typ av bindningar deltar sidogrupperna hos polära aminosyror?\nDe kan bilda vätebindingar med vatten eller andra polära molekyler.\n#### Vilka aminosyror är basiska?\nLysin och Arganin\n#### Vilka egenskaper har basiska aminosyror?\nDe är känsliga för pH-ändringar, har en netto positiv laddning, vattenlösliga och kan ta upp protoner\n\n#### I vilken typ av bindningar deltar sidogrupperna hos basiska aminosyror?\nVätebindingar och jonladdningar (saltbryggor)\n#### Vilka aminosyror är sura?\nAspartat och glutamat\n#### Vilka egenskaper har sura aminosyror?\nHydrofila och har karboxylgrupper i kedjan som gör att de kan avge protoner vilket ger dem en negativ laddning vid fysiologiskt pH\n#### I vilken typ av bindningar deltar sidogrupperna hos sura aminosyror?\nVätebindingar och jonladdningar (saltbryggor)\n#### Vilka aminosyror har sidogrupper som kan ändra laddning beroende på pH?\nXXX: för svårt just nu\n#### Hur bildas en peptidbindning?\nVia kondensering skapas en aminbindning mellan första aminosyrans aminogrupp och den andras karboxylgrupp, detta avger vatten\n#### Vad karaktäriserar en peptidbindning?\nDen har:\n- delvis dubbelbindningkaraktär som gör den rak och stel\n- delvis resonansstabilisering mellan C=O och C-N vilket gör den starkare än en enkelbindning\n#### Vad är primärstruktur?\nEn linjär sekvens av aminosyror, även kallad en peptidkedja\n#### Vad menas med att en peptidkedja har en riktning?\nDen första aminosyran där en peptidkedja börjar kallas N-terminal, den har bara en peptidbindning på karboxylgruppen, aminogruppen saknar det.\nDen sista aminosyran där en peptidkedja slutar C-terminal, den har bara en peptidbinding på aminogruppen, karboxylgruppen saknar det.\nRiktningen går ifrån N-terminal till C-terminal.\n#### Vilken är skillnaden mellan en cis- och en transkonfiguration hos en polypeptidkedja?\nPeptidbindningen är stel och kan inte rotera, men det kan alfakolet som antingen kan roteras i cis- eller trans-konfiguration.\nI cis så ligger de två alfakolen på samma sida\nI trans ligger det på motsatta sidor\n#### Vad är sekundärstruktur?\nDen lokala 3D-strukturen hos en peptidkedja, finns tre typer a-helix, hårnålsböj eller b-flak. #### Vad karaktäriserar en a-helix?\nDet är en stabil, spiralformad struktur där diametern är konstant. Varje vätebindning sitter mot 4 aminosyror framemot med en genomsnittslig varv på 3.6 aminosyror.\n#### Vilken typ av bindningar stabiliserar sekundärstrukturen a-helix och vilka delar av aminosyrorna förbinds?\nDe stabiliseras av vätebindningar mellan karboxylgruppen (-C=O) och aminogruppen (-N-H).\n#### Vilken sekundärstruktur finns ofta när en polypeptidkedja byter riktning och hur är den uppbyggd?\nDå bildas ofta en hårnålsböj som består vanligtvis av fyra aminosyror där prolin ofta orsakar böjen och glycin bidrar med flexibilitet.\n -Subsystem: com.intellij.openapi.diff.impl.patch.CharsetEP -<+>UTF-8 -=================================================================== -diff --git a/content/Biokemi/Från aminosyror till proteiner/Frågeställning I.md b/content/Biokemi/Från aminosyror till proteiner/Frågeställning I.md ---- a/content/Biokemi/Från aminosyror till proteiner/Frågeställning I.md (revision 2c6d179b83818982e44d26cf654aefd3247c0e51) -+++ b/content/Biokemi/Från aminosyror till proteiner/Frågeställning I.md (date 1762453127412) -@@ -97,3 +97,19 @@ - De stabiliseras av vätebindningar mellan karboxylgruppen (-C=O) och aminogruppen (-N-H). - #### Vilken sekundärstruktur finns ofta när en polypeptidkedja byter riktning och hur är den uppbyggd? - Då bildas ofta en hårnålsböj som består vanligtvis av fyra aminosyror där prolin ofta orsakar böjen och glycin bidrar med flexibilitet. -+ -+#### Vad är tertiärstruktur? -+#### Vad gör att proteiner vanligtvis veckas rätt? -+#### Vad innebär isoelektrisk punkt för ett protein? -+#### Vilka bindningar bidrar till att stabilisera tertiärstrukturen hos ett globulärt cytoplasmatiskt protein? -+#### Vilka typer av proteiner kan hjälpa andra proteiner att veckas? Varför är det viktigt att proteiner som veckats fel får hjälp att veckas rätt? -+#### Vad är kvartärstruktur? -+#### Vilken aminosyra kan bidra till att stabilisera såväl tertiär som kvartärstruktur genom att -+#### bilda kovalenta bindningar och hur är de bindningarna uppbyggda? -+#### Vad karaktäriserar proteiner som kan ha två olika strukturer? -+#### Vad innebär det att ett protein denatureras? -+#### Vad kan få ett protein att denatureras? -+#### Vad är en proteindomän? -+#### Vad är en subenhet och hur namnges proteinsubenheter? -+#### Hur mäts proteiners massa? -+#### Vilket är sambandet mellan proteinveckning och amyloider? -\ No newline at end of file -Index: content/.obsidian/workspace.json -IDEA additional info: -Subsystem: com.intellij.openapi.diff.impl.patch.BaseRevisionTextPatchEP -<+>{\n \"main\": {\n \"id\": \"19179b278823b064\",\n \"type\": \"split\",\n \"children\": [\n {\n \"id\": \"eb22729992e774cb\",\n \"type\": \"tabs\",\n \"children\": [\n {\n \"id\": 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b/content/Biokemi/Proteinseminarie/Frågor.md index 8e66511..e3a4175 100644 --- a/content/Biokemi/Proteinseminarie/Frågor.md +++ b/content/Biokemi/Proteinseminarie/Frågor.md @@ -28,10 +28,16 @@ Resultatet är **högerförskjuten dissociationskurva**, lägre O₂-bindning oc ### Blodgrupper En lyckad transfusion av blod från en individ till en annan är beroende av att individerna har kompatibla blodgrupper. Om blodgrupperna inte är kompatibla kan en livshotande reaktion utlösas. Redogör för reaktionen för molekylär nivå. +Vid inkompatibel blodtransfusion känns mottagarens antikroppar igen donatorns erytrocytantigen (t.ex. A- eller B-antigen) som främmande. Antikropparna binder direkt till antigenen på erytrocyterna och bildar stora immunkomplex. Detta leder till **agglutination** (klumpning) och aktivering av **komplementsystemet**, som skapar porer i cellmembranet och orsakar **intravaskulär hemolys**. Frisatta hemoglobinfragment och komplementaktiverade mediatorer utlöser kraftig inflammation, kärlskada, koagulationsaktivering och kan snabbt leda till chock, njursvikt och cirkulationskollaps. ### Enzymer Redogör för fördelen med att många enzymer har Km-värden i närheten av de substratkoncentrationer som finns i deras omgivning. -### +När ett enzyms Km ligger nära den faktiska substratkoncentrationen fungerar enzymet i det mest känsliga området av Michaelis-Menten-kurvan. Det innebär att små förändringar i substratnivåer direkt ger tydliga förändringar i hastigheten, vilket gör enzymet finreglerbart och responsivt. Enzymet arbetar varken mättat eller ineffektivt, utan i ett dynamiskt intervall där cellen snabbt kan anpassa metabolismen efter behov. Detta gör att enzymaktivitet kan styras av tillgången på substrat utan att kräva stora mängder enzym eller komplex reglering. +### Kofaktorer Kofaktorer bundna till proteiner är viktiga för att möjliggöra vissa kemiska reaktioner och därmed utöka repertoaren av reaktioner de kan utföra. Redogör för vad en kofaktor är och hur kofaktorerna ... kan hjälpa enzymer att uppnå effektivitet i de reaktioner de katalyserar. -Förklara hur förtäring av metanol kan ge svåra förgiftningsskador samt hur etanol kan förhindra förgiftningen. \ No newline at end of file +Kofaktorer är små icke-proteinkomponenter som ett enzym behöver för att katalysera reaktioner som aminosyror själva inte klarar av. De kan vara **metalljoner** (t.ex. Zn²⁺, Mg²⁺, Fe²⁺) eller **organiska molekyler** som ofta kallas **coenzymer** (t.ex. NAD⁺, FAD, CoA, TPP, biotin). Kofaktorer kan bära elektroner, protoner eller kemiska grupper, stabilisera övergångstillstånd eller skapa reaktiva intermediärer. Genom att tillföra nya kemiska egenskaper – redoxförmåga, gruppöverföring, syra–bas-katalys eller strukturell stabilisering – ökar de både reaktionshastighet och specificitet och gör att enzymet kan utföra reaktioner som annars vore omöjliga. +### Metanol +Förklara hur förtäring av metanol kan ge svåra förgiftningsskador samt hur etanol kan förhindra förgiftningen. + +Metanol i sig är relativt ofarligt, men i levern omvandlar **alkoholdehydrogenas (ADH)** det till **formaldehyd** och vidare till **myrsyra**, vilket orsakar **metabol acidos**, synnervsskada och kan leda till blindhet och död. Etanol fungerar som behandling eftersom ADH har **mycket högre affinitet för etanol än metanol**. När etanol ges konkurrerar det ut metanol på enzymet, vilket stoppar bildningen av de toxiska metaboliterna. Metanol utsöndras då oförändrat och myrsyran kan metaboliseras eller buffras. \ No newline at end of file diff --git a/content/Biokemi/Proteinseminarie/Stödord.md b/content/Biokemi/Proteinseminarie/Stödord.md index c44524f..2863c86 100644 --- a/content/Biokemi/Proteinseminarie/Stödord.md +++ b/content/Biokemi/Proteinseminarie/Stödord.md @@ -1,17 +1,11 @@ -**Polaritet** -- skillnad i laddning / vätebindning -- elektronegativitet (O/N eller mättat kol) -**Driver struktur** -- hydrofob effekt -- ficka, disulfid/ -- pol-mutationer → HbS - - | Nummer | | | | ------ | --------------------- | ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- | -| 1 | Aminosyrors polaritet | - skillnad i laddning / vätebindning
- elektronegativitet: O/N el mättat kol
- hydrofob effekt
- ficka, disulfid/H-/jon-
- pol-mutationer → HbS | +| 1 | Aminosyrors polaritet | skillnad i laddning / vätebindning
elektronegativitet: O/N el mättat kol
hydrofob effekt
ficka, disulfid/H-/jon-
polaritetmutationer → HbS | | 2 | Aminosyrors veckning | påverkas av: R-pol, H-, hinder,
AF tränad, proteiner, 3D vinklar, avstånd | | 3 | Proteinanalys | Jonbytes: laddning, res euleras via salt/pH
Gelfil: storlek, stora i porer, små går runt
elektrofores: storlek+laddning, bryter ner 3D
friktion, redu-medel för disulfidbryggor | -| 4 | Hb | - ↓O₂ → T-state
- ↑CO₂/H⁺ → nya saltbryggor, stänger, O2 svårare att binda
- CO₂ → karbamat
- högerförskjutning | -| 5 | Blodgrupper | | +| 4 | Hb | ↓O₂ → T-state
↑CO₂/H⁺ → nya saltbryggor, stänger, O2 svårare att binda
CO₂ → karbamat
högerförskjutning | +| 5 | Blodgrupper | inkomp = Ab + Ag
agglutination
komplement → porer
hemolys
Hb + inflammation
chock / njure / koag | +| 6 | Enzymer | Km ≈ [S]
känslighet
snabb reglering
ej mättat
dynamiskt område | +| 7 | Kofaktorer | metaller / coenzym
bär elektroner / grupper
stabiliserar TS
ökad hastighet & specificitet | +| 8 | Metanol | metanol → formaldehyd → myrsyra
acidos + synnerv
etanol konkurrerar ADH |