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Introduction to Thermodynamics and Biochemistry: Gibbs Free Energy, Proteins, and Buffers, Quizzes of Social Anthropology

Definitions and explanations of key concepts related to gibbs free energy, including delta g, delta h, delta s, standard gibbs energy, and the role of gibbs free energy in making unfavorable reactions favorable. The document also covers the hydrolysis of atp, amphipathic molecules, acids and bases, buffer effect, and the structure and function of amino acids and proteins. Terms related to protein structure, including primary, secondary, tertiary, and quaternary structures, are also discussed.

Typology: Quizzes

2013/2014

Uploaded on 09/23/2014

rachelazamora
rachelazamora 🇺🇸

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Download Introduction to Thermodynamics and Biochemistry: Gibbs Free Energy, Proteins, and Buffers and more Quizzes Social Anthropology in PDF only on Docsity! TERM 1 Gibbs Free Energy DEFINITION 1 delta G= deltaH - TdeltaS TERM 2 G* DEFINITION 2 gibbs free energy at STANDARD CONDITIONS TERM 3 delta H DEFINITION 3 Enthalpythe energy stored in a bond = + positivethe energy released = - negativeheat released TERM 4 Delta S DEFINITION 4 Enthalpymeasure of disorganizationfavorable = +positive = more disordernegative - = less disorder TERM 5 Standard Gibbs Energy Equation DEFINITION 5 delta G* = - RT ln Keq TERM 6 R= DEFINITION 6 8.314 J/mol * K TERM 7 Standard Condition DEFINITION 7 1 atm25*C = 298 K1 Molar Product & Reactants TERM 8 Gibbs when not at standard conditions equation DEFINITION 8 delta G = G* + RT ln QQ= [Products]/ [Reactants] at moment not at equilibrium TERM 9 How to make unfavorable reactions favorable? DEFINITION 9 -change concentrations-couple unfavorable with extremely favorable reactions to make a relatively favorable reaction TERM 10 ATP hydrolysis DEFINITION 10 ATP --> ADP + Pioccurs when you add H20FAVORABLE TERM 21 Zwitterion DEFINITION 21 neutral molecule with positive and negative charge to make neutral compound TERM 22 All Amino Acids are ________ DEFINITION 22 L - stereoisomers TERM 23 Structure of AA DEFINITION 23 Amino groupCarboxylic AcidHydrogen = into the boardSide Chain R = out of the board TERM 24 pKa of amino group DEFINITION 24 9.5 TERM 25 pKa of carboxylic acid DEFINITION 25 2.2 TERM 26 Essential Amino Acids DEFINITION 26 not in diet!ValineIsoleucineLeucineMethionineTryptophanPhenylalanineHistidineThreonineLysine TERM 27 Small Hydrophobic DEFINITION 27 GlycineAlanineValineIsoleucineLeucineProlineMethionine TERM 28 Big and Bulky AA DEFINITION 28 TryptophanPhenylalanineTyrosine TERM 29 Alcohol / Thiol DEFINITION 29 SerineThreonineCystine TERM 30 Polar/ Acidic DEFINITION 30 AsparagineAspartic AcidGlutanamineGlutamic Acid TERM 31 Base / Buffer DEFINITION 31 LysineArginineHistidine TERM 32 Peptide Bond DEFINITION 32 covalent bond when carboxyl group binds with an amino groupthis forms resonance TERM 33 Sequence of Proteins DEFINITION 33 only points of flexibility are at alpha carbons TERM 34 Primary Structure DEFINITION 34 sequence of amino acids TERM 35 Motifs DEFINITION 35 sequence of amino acids for a common purposespecific conserved sequence TERM 46 Super Secondary Structure (2) DEFINITION 46 2) Helix-turn- Helix2 alphas joined by turnmajor way proteins "READ" DNAone helix fits into the major groove of DNA, the other helix helps position first TERM 47 Primary structure is ____ DEFINITION 47 linear TERM 48 Secondary structure have proteins interact via ____ DEFINITION 48 backbone TERM 49 Tertiary Structure DEFINITION 49 AlphaBetaAlpha-Beta TERM 50 Describe tertiary structures DEFINITION 50 determines interactionsinternal AA are hydrophobicexternal AA are hydrophilicloops tend to be hydrophilic TERM 51 Tertiary structure is sealed by... DEFINITION 51 SALT BRIDGESDISULFIDE BONDSMETAL IONS TERM 52 can tertiary structures be undone? DEFINITION 52 YESbecause not covalent bondsmay be undone & denatured TERM 53 How to denature? DEFINITION 53 temperaturepHovercoming "hydrophobic effect" via detergents, via chaotropic agents TERM 54 Chaotropic Agents DEFINITION 54 disrupt H bonding between H20 moleculesex: Urea TERM 55 Quaternary Structures DEFINITION 55 multiple proteins coming togetherEach step exists in equilibriumsome proteins function at semi-folded state TERM 56 Energetics DEFINITION 56 random coil = most disorder/ highest Energy*LOOK AT NOTEBOOK* TERM 57 Protein folding goes wrong/ doesn't work DEFINITION 57 unfolded protein can start to interact with other polypeptide chains instead of another alpha helixAmyloid Fibers: form plaques =bacteria use this strategy to grow its own surfaceForm long folds of protein B sheetsOut of Control= DISEASE TERM 58 Disease caused by incorrect protein folding DEFINITION 58 ALSAlzheimersParkinsons TERM 59 Ligand DEFINITION 59 molecule with which a protein specifically interacts TERM 60 Domain DEFINITION 60 two sets in tertiary structure of a protein
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