BIO 205 Study Guide - Midterm Guide: Fetus, Linus Pauling, Asparagine

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coralwhale510

21 Mar 2018

School

University at Buffalo

Department

Biological Sciences

Course

BIO 205

Professor

Snyder Grayson

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Document Summary

Residues: four levels of structures, primary: sequence of amino acids, not altered by urea. 3: secondary: helices and sheets; h-bonding between backbone groups, phi and psi angles, tertiary: 3-dimensional folding, quaternary: relationships in multi-chain proteins; subunits, b-mercaptoethanol denatures some proteins by reducing. Sh groups: urea denatures proteins by breaking h-bonds, both in. Proteins and in organized solvent lattices: carbonyl groups participate in h bonds of the alpha helix. In the first four residues at the n-terminus of the helix: pro and gly both disfavor helix formation, in an alpha helix, the r group (sidechain) resides on the. Outside of the helix spiral: linus pauling published a model with a left-handed spiral. Instead of a right handed spiral: peptide bond: a bond exhibiting restricted rotation, protein denaturation: unfolding of the compact native. Conformation of each chain: unfavorable protein, favorable effect for the solvent, ramachandran plots sterically permitted rotational.

Related Questions

Why are there amino acids and fatty acids designated as essential?

Basic proteins cannot be made without essential amino acids

Essential amino acids are water soluble; therefore they need to be ingested every day

Essential fatty acids are lipid soluble (able to be stored); therefore we wonât run out of them

Essential amino acids cannot be synthesized by enzymatic reactions

Predict what amino acids line the inner channel of a protein that transports protons (H⁺) across membranes compared to the inner channel of a protein that transports a negatively charged substance across membranes.

A.Both channels are lined with hydrophobic amino acids

B.Both channels are lined with hydrophilic amino acids

C.The H⁺ transporterâs inner channel is lined with hydrophobic amino acids; the other transport proteinâs inner channel is lined with hydrophilic amino acids.

D.The H⁺ transporterâs inner channel is lined with hydrophilic amino acids; the other transport protein is lined with hydrophobic amino acids.

E.One cannot answer this question without knowing what the other transported substance is.

blackmule728

Look at your table of amino acid R-group structures. Which category amino acids are likely to change physical and/or chemical properties if the pH of the surrounding medium changes?

Polar, non charged amino acids.

Basic amino acids.

Non-polar amino acids.

Look at your amino acid structure tables. What category of amino acid is histidine?

basic

non-polar

polar, non-charged

How would Bronsted-Lowry describe histidine?

proton acceptor

proton donor