Lecture 5 protein structure and function

<p>Their specific three-dimensional structure (A)</p> Signup and view all the answers

<p>The role of proteins (B)</p> Signup and view all the answers

<p>Misfolded proteins (D)</p> Signup and view all the answers

<p>Peptide bond (B)</p> Signup and view all the answers

<p>Ribosomes (C)</p> Signup and view all the answers

<p>Oligopeptide (B)</p> Signup and view all the answers

<p>Alternating position along the backbone (A)</p> Signup and view all the answers

<p>Nuclear magnetic resonance (NMR) spectroscopy (A)</p> Signup and view all the answers

<p>It reduces computational time significantly. (A)</p> Signup and view all the answers

<p>Antiparallel β sheets are more common in proteins. (A)</p> Signup and view all the answers

<p>PubMed (A)</p> Signup and view all the answers

<p>It can reveal the protein's function and how it works. (D)</p> Signup and view all the answers

<p>Secondary structure. (A)</p> Signup and view all the answers

<p>In a quick reference guide. (A)</p> Signup and view all the answers

<p>Interactions between the side chains of amino acid residues. (A)</p> Signup and view all the answers

<p>Disulfide bonds. (B)</p> Signup and view all the answers

<p>The disulfide bonds will break and the structure may be altered. (B)</p> Signup and view all the answers

<p>To the C-terminus (A)</p> Signup and view all the answers

<p>Hydrogen bonds between backbone constituents (A)</p> Signup and view all the answers

<p>A right-handed coil (C)</p> Signup and view all the answers

<p>Alpha (α) helix (D)</p> Signup and view all the answers

<p>Unstructured regions (C)</p> Signup and view all the answers

<p>Due to hydrogen bonding along the backbone (D)</p> Signup and view all the answers

<p>Asparagine and glutamine have amide groups, while aspartate and glutamate have carboxyl groups on their side chains. (B)</p> Signup and view all the answers

<p>Coiled-coil (A)</p> Signup and view all the answers

<p>Phosphorylation introduces a bulky, highly negative charge, altering ionic and polar interactions. (D)</p> Signup and view all the answers

<p>The amino-terminus and carboxy-terminus (B)</p> Signup and view all the answers

<p>They have hydroxyl groups capable of hydrogen bonding. (D)</p> Signup and view all the answers

<p>Its thiol group. (C)</p> Signup and view all the answers

<p>Ionic bonds with positively charged (basic) residues, and other ionized molecules. (B)</p> Signup and view all the answers

<p>By interacting with the positive dipoles of water and other molecules. (B)</p> Signup and view all the answers

<p>By forming ionic bonds and dipole interactions within a polypeptide. (B)</p> Signup and view all the answers

<p>Through the attraction and repulsion of different protein domains. (A)</p> Signup and view all the answers

Proteins are dynamic molecules driving biological activity through interactions.

Carbohydrates store energy and provide structural support in cells.

Lipids store energy, provide cushioning, and form cell membranes.

DNA stores genetic information; RNA assists in gene expression and has other functions.

The function of proteins is tightly linked to their structure.

Proteins that have not folded into their correct shape, potentially losing function.

The unique sequence of amino acids in a polypeptide, encoded in DNA.

A covalent bond formed between two amino acids when they join.

A secondary structure in proteins characterized by rigid folding patterns.

The most common form of β sheets where adjacent strands run in opposite directions.

A molecule formed from two amino acids linked by a peptide bond.

A long chain of amino acids (many residues) forming a protein.

Insulin-like aggregates of β sheets linked to neurodegenerative diseases.

3D shape of a protein formed by interactions among amino acid side chains.

Covalent bonds between cysteine residues that stabilize protein structure.

Amino acids similar to aspartate and glutamate, with amide side chains.

The addition of a phosphate group to amino acids, affecting protein function.

Amino acids that interact well with water due to polar side chains.

An amino acid containing a thiol group important for protein structure.

Amino acids with additional carboxylic groups, typically negatively charged in cells.

Amino acids with nitrogenous groups that can form ionic bonds and enhance solubility.

The process of polypeptides folding into their lowest energy conformation during synthesis.

Water influences the conformation and stability of protein structures.

Flexible parts of the polypeptide that do not have a defined structure, found between structured regions.

Regions of the polypeptide chain that are stabilized by hydrogen bonds, forming coils or folds.

A right-handed coil formed by hydrogen bonds in a polypeptide's secondary structure.

A sheet-like structure formed by hydrogen bonding between segments of a polypeptide chain.

Proteins that often cross the lipid bilayer as α helices, functioning as enzymes or receptors.

A structure formed by intertwined α helices that creates a stiff, elongated protein.

Weak interactions that stabilize the secondary structure of proteins, connecting parts of the polypeptide backbone.

A spectroscopy method for investigating protein structure without crystallization, but less informative.

The use of computational tools to predict protein structures from amino acid sequences, needing high computing power.

AI significantly speeds up the computation in bioinformatics, improving efficiency in predicting protein structures.

Proteins have four structural levels: primary, secondary, tertiary, and quaternary, each affecting functionality.

The specific structure of a protein dictates its function within biological systems, essential for understanding biology.