BIO 101 Lecture Notes - Lecture 3: Glutamine, Hydrophile, Phenylalanine

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lemondinosaur366

3 Nov 2016

School

Quinnipiac University

Department

Biology

Course

BIO 101

Professor

Holdaway

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Document Summary

Amino acid structure: all amino acids have an amino and carboxyl (acid) attached to a central carbon with hydrogen. Amino acids serve as weak acids (protein donors) and weak bases (proton acceptors) Protein: in every living thing/organism, every proteins are made of the 20 amino acids. Everything is made up of the same things. Peptide bond = bond between amino acids. Ala, val, leu, ile, pro, phe, trp, met. Gly, ser, thr, cys, tyr, ash, gln. Lys, arg, his: non-polar hydrophobic, polar hydrophilic (non-charged, acidic negatively charged, basic positively charged. Carbohydrates, lipids and proteins linked the same way dehydrations. Protein = long chain of amino acids aka primary structure. Each protein has a different sequence of amino acids synthesis. Hydrophilic amino acids are attracted to other hydrophilic substances, and hydrophobic are not. N-h bonds to o=c = hydrogen bond holds helix together. (beta) pleated sheet held together by hydrogen bonds.

Related Questions

Alpha helices and beta sheets have common structural motifs but can contain very different amino acid sequences. For each of the following, circle the correct structure that could form given that sequence.

A. phe-leu-val-gly-ser-phe-leu-tyr-leu-gly-met-trp-leu-leu-phe-ile

amphipathic a helix hydrophilic a helix hydrophobic a helix

B. Ile-ala-asn-thr-leu-gly-thr-ala-ile-gln-ser-ile-ala-cys-leu-leu

amphipathic a helix hydrophilic a helix hydrophobic a helix

C. ser-ile-gln-leu-thr-phe-asn-met-glu-ile-glu-ala-thr-ile-arg-phe

amphipathic b sheet hydrophilic b sheet hydrophobic b sheet

D. asn-thr-asp-ser-tyr-asp-met-thr-ser-his-thr-asn-leu-lys-thr-ser

amphipathic b sheet hydrophilic b sheet hydrophobic b sheet

For the following strand of DNA, use the table below to provide: bases for the complementary mRNA and the associated amino acids. What do you notice about the genetic code for proline in the peptide? How would the loss of the first G or switching that G to a T affect the structure and function of this protein?

DNA: GGC CTA CAA GCC GGA ACA GTT ACC GCG TAA CGA

RNA: ??? ??? ??? ??? ??? ??? ??? ??? ??? ??? ???

Amino Acid:??? ??? ??? ??? ??? ??? ??? ??? ??? ??? ???
(3 Letters)

Genetic Code Table (mRNA)

1st position (5' end)	2nd position (middle)				3rd position (3' end)
1st position (5' end)	U	C	A	G	3rd position (3' end)
U	Phe F Phe F Leu L Leu L	Ser S Ser S Ser S Ser S	Tyr Y Tyr Y STOP STOP	Cys C Cys C STOP Trp W	U C A G
C	Leu L Leu L Leu L Leu L	Pro P Pro P Pro P Pro P	His H His H Gln Q Gln Q	Arg R Arg R Arg R Arg R	U C A G
A	Ile I Ile I Ile I Met M	Thr T Thr T Thr T Thr T	Asn N Asn N Lys K Lys K	Ser S Ser S Arg R Arg R	U C A G
G	Val V Val V Val V Val V	Ala A Ala A Ala A Ala A	Asp D Asp D Glu E Glu E	Gly G Gly G Gly G Gly G	U C A G

turquoisewater-buffalo47

Please help me with this question,

1. At pH 7.0, in what order would the following three peptides be eluted from a column filled with an anion-exchange polymer? Their amino acid compositions are:

Peptide A: Ala 10%, Glu 5%, Ser 5%, Leu 10%, Arg 10%, His 5%, Ile 10%, Phe 5%, Tyr 5%, Lys 10%, Gly 10%, Pro 5%, and Trp 10%.

Peptide B: Ala 10%, Glu 10%, Gly 5%, Leu 5%, Asp 10%, Arg 5%, Met 5%, Cys 5%, Tyr 5%, Phe 5%, His 5%, Val 5%, Pro 5%, Thr 5%, Ser 5%, Asn 5%, and Gln 5%.

Peptide C: Ala 5%, Val 5%, Gly 10%, Asp 5%, Leu 5%, Arg 5%, Ile 5%, Phe 5%, Tyr 5%, Lys 5%, Trp 5%, Ser 5%, Thr 5%, Glu 5%, Asn 5%, Pro 10%, Met 5%, and Cys 5%.

First off column: _______________ Second: _______________ Last off column: _______________

BIO 101 Lecture Notes - Lecture 3: Glutamine, Hydrophile, Phenylalanine

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