MCBG 2 - Proteins at University Of Leicester | Flashcards & Summaries

Select your language

Suggested languages for you:
Log In Start studying!

Lernmaterialien für MCBG 2 - Proteins an der University of Leicester

Greife auf kostenlose Karteikarten, Zusammenfassungen, Übungsaufgaben und Altklausuren für deinen MCBG 2 - Proteins Kurs an der University of Leicester zu.

TESTE DEIN WISSEN

Which amino acid end corresponds to which terminal?

Lösung anzeigen
TESTE DEIN WISSEN

NH3+ is at N-terminal end

COO- is at C-terminal end

Lösung ausblenden
TESTE DEIN WISSEN

What is the isoelectric point?

Lösung anzeigen
TESTE DEIN WISSEN

The isoelectric point (pI) of a protein is the pH at which there is no overall net charge (the number of NH3+ and COO- along with any other charges balance out).

Lösung ausblenden
TESTE DEIN WISSEN

How are proteins classified?

Lösung anzeigen
TESTE DEIN WISSEN

They are classified according to chemical or physical properties of the R groups.

Chemical

  • Hydrophilic/Hydrophobic
  • Polar/Non polar
  • Acidic/Basic

Physical

  • Aliphatic
  • Aromatic
Lösung ausblenden
TESTE DEIN WISSEN

Key features of proteins.

Lösung anzeigen
TESTE DEIN WISSEN
  • Complex
  • Highly specific
  • Three-dimensional structure

The folding of proteins depends on the chemical and physical properties of the amino acids.

Lösung ausblenden
TESTE DEIN WISSEN

Describe each type of structure of proteins.

Lösung anzeigen
TESTE DEIN WISSEN

Primary 

  • Linear amino acid chain

Secondary 

  • Spatial arrangement of polypeptide backbone
  • e.g. helices or beta sheets

Tertiary 

  • The 3-dimensional configuration of the protein

Quaternary

  • Association of more than one polypeptide
  • Form a multi-subunit protein
  • e.g. antibodies, ribosomes, haemoglobin
Lösung ausblenden
TESTE DEIN WISSEN

Features of a peptide bond.

Lösung anzeigen
TESTE DEIN WISSEN

Covalent bond between amino acids.

Formed by hydrolysis - H20 removed

Peptide bonds are (trigonal) planar around the carboxyl carbon

Rigid - little rotation

Adopt a trans conformation (opposite sides)

Partial double bond characteristics

Lösung ausblenden
TESTE DEIN WISSEN

Compare globular and fibrous proteins.

Lösung anzeigen
TESTE DEIN WISSEN

Globular

  • Compact structure
  • Various types of secondary structures
  • e.g. enzymes

Fibrous 

  • Extended / elongated
  • Single type of repeating secondary structures
  • e.g. collagen made up of triple helical structure
Lösung ausblenden
TESTE DEIN WISSEN

How do chemical properties affect folding of protein?

Lösung anzeigen
TESTE DEIN WISSEN

Hydrophobic / non-polar side chains are buried  inwards and hydrophilic / polar / charged chains are on the surface to allow for interactions with aqueous surroundings.

Lösung ausblenden
TESTE DEIN WISSEN

Why can protein misfolding have severe effects?

Lösung anzeigen
TESTE DEIN WISSEN

Altered conformation  of a normal human protein due to misfolding converts existing protein into diseased state.

  • e.g. amyloid fibres are a misfolded insoluble form of a normally soluble protein
Lösung ausblenden
TESTE DEIN WISSEN

What is a zwitterion and why is it relevant in protein structure?

Lösung anzeigen
TESTE DEIN WISSEN

A molecule containing both positive and negative moiety's. At most pH's (3-9), proteins have both +ve and -ve moiety's 

  • R--NH3+
  • R--COO-
Lösung ausblenden
TESTE DEIN WISSEN

Outline the process of protein folding.

Lösung anzeigen
TESTE DEIN WISSEN
  • Localised areas fold to maintain stable conformations
  • Driven by the need to find most stable conformation
  • Until the whole protein is folded 
  • The folding is determined by the amino acid sequence
Lösung ausblenden
TESTE DEIN WISSEN

What is an amino acid residue?

Lösung anzeigen
TESTE DEIN WISSEN

The structure of an amino acid after  it has formed a peptide bond with other amino acids to form a protein (H2O is lost).

Lösung ausblenden
  • 1695 Karteikarten
  • 170 Studierende
  • 0 Lernmaterialien

Beispielhafte Karteikarten für deinen MCBG 2 - Proteins Kurs an der University of Leicester - von Kommilitonen auf StudySmarter erstellt!

Q:

Which amino acid end corresponds to which terminal?

A:

NH3+ is at N-terminal end

COO- is at C-terminal end

Q:

What is the isoelectric point?

A:

The isoelectric point (pI) of a protein is the pH at which there is no overall net charge (the number of NH3+ and COO- along with any other charges balance out).

Q:

How are proteins classified?

A:

They are classified according to chemical or physical properties of the R groups.

Chemical

  • Hydrophilic/Hydrophobic
  • Polar/Non polar
  • Acidic/Basic

Physical

  • Aliphatic
  • Aromatic
Q:

Key features of proteins.

A:
  • Complex
  • Highly specific
  • Three-dimensional structure

The folding of proteins depends on the chemical and physical properties of the amino acids.

Q:

Describe each type of structure of proteins.

A:

Primary 

  • Linear amino acid chain

Secondary 

  • Spatial arrangement of polypeptide backbone
  • e.g. helices or beta sheets

Tertiary 

  • The 3-dimensional configuration of the protein

Quaternary

  • Association of more than one polypeptide
  • Form a multi-subunit protein
  • e.g. antibodies, ribosomes, haemoglobin
Mehr Karteikarten anzeigen
Q:

Features of a peptide bond.

A:

Covalent bond between amino acids.

Formed by hydrolysis - H20 removed

Peptide bonds are (trigonal) planar around the carboxyl carbon

Rigid - little rotation

Adopt a trans conformation (opposite sides)

Partial double bond characteristics

Q:

Compare globular and fibrous proteins.

A:

Globular

  • Compact structure
  • Various types of secondary structures
  • e.g. enzymes

Fibrous 

  • Extended / elongated
  • Single type of repeating secondary structures
  • e.g. collagen made up of triple helical structure
Q:

How do chemical properties affect folding of protein?

A:

Hydrophobic / non-polar side chains are buried  inwards and hydrophilic / polar / charged chains are on the surface to allow for interactions with aqueous surroundings.

Q:

Why can protein misfolding have severe effects?

A:

Altered conformation  of a normal human protein due to misfolding converts existing protein into diseased state.

  • e.g. amyloid fibres are a misfolded insoluble form of a normally soluble protein
Q:

What is a zwitterion and why is it relevant in protein structure?

A:

A molecule containing both positive and negative moiety's. At most pH's (3-9), proteins have both +ve and -ve moiety's 

  • R--NH3+
  • R--COO-
Q:

Outline the process of protein folding.

A:
  • Localised areas fold to maintain stable conformations
  • Driven by the need to find most stable conformation
  • Until the whole protein is folded 
  • The folding is determined by the amino acid sequence
Q:

What is an amino acid residue?

A:

The structure of an amino acid after  it has formed a peptide bond with other amino acids to form a protein (H2O is lost).

MCBG 2 - Proteins

Erstelle und finde Lernmaterialien auf StudySmarter.

Greife kostenlos auf tausende geteilte Karteikarten, Zusammenfassungen, Altklausuren und mehr zu.

Jetzt loslegen

Das sind die beliebtesten MCBG 2 - Proteins Kurse im gesamten StudySmarter Universum

Proteins

Middlesex University

Zum Kurs
Proteins

Mindanao State University - Iligan Institute of Technology

Zum Kurs
PROTEIN (MIDTERM)

Our Lady of Fatima University

Zum Kurs
Proteine

Justus-Liebig-Universität Gießen

Zum Kurs
CCLAB PROTEINS

Saint Louis College

Zum Kurs

Die all-in-one Lernapp für Studierende

Greife auf Millionen geteilter Lernmaterialien der StudySmarter Community zu
Kostenlos anmelden MCBG 2 - Proteins
Erstelle Karteikarten und Zusammenfassungen mit den StudySmarter Tools
Kostenlos loslegen MCBG 2 - Proteins