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BIO-309

BIOCHEMISTRY I

IV. WEEK

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LECTURE CONTENTS OF 4TH WEEK

• Continue to the Peptides and Proteins

• Oligopeptide, polypeptide, amino and carboxyl end, oligomeric, protomer, conjugated protein, prosthetic group, examples, polymorphic, proteomic,

bioinformatics concepts will be discussed.

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•The description of the requirements for the

conversion of amino acid

sequences in a polypeptide

chain to a three-dimensional

structure will begin from this

lecture.

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• 1-The three-dimensional structure of a protein is determined by the amino acid sequences

• 2-The function of a protein depends on its structure

• 3-The protein isolated from any

source usually has one or more

stable structural states

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•4-The most important power that stabilizes the proteins is their non-covalent

interactions

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•5-Finally, the architectural

properties of proteins needs

to be determined to perform

their functions. This topic will

provide general information

about protein architecture.

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•Secondary structure of proteins: The concept of peptide bond forming

secondary structure, its

properties, Ramachandran

graphics, α-helical structure, β-turns and β-sheet

structures will be discussed,

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https://www.google.com/url?sa=i&url=https%3A%2F%2Fpt.slideshare.net

%2FSabahatAli9%2Fprotein-structure-

levels&psig=AOvVaw0yeZf52cOtXPLUulsnHZ5H&ust=1589380255496000&source=images&cd=

vfe&ved=0CAIQjRxqFwoTCJjJ_f7ErukCFQAAAAAdAAAAABAo

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https://www.google.com/url?sa=i&url=https%3A%2F%2Fwww.onlinebiologynotes.com%2Fpeptide-types-functions

%2F&psig=AOvVaw3R_C9X_b-

_Nf1jWPv6xyHw&ust=1589381725227000&source=images&cd=vfe&ved=0CAIQjRxqFwoTCPiY6b3KrukCFQAAA AAdAAAAABAD

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• Possible conformation of proteins

can be found in a different structural state without covalent bonds being touched.

• A protein containing a large number of single bonds may theoretically be present in hundreds of different

conformation.

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https://www.google.com/url?sa=i&url=https%3A%2F%2Fhudabeauty.com%2Fus%2Fen_US%2Fblog%2Fpeptides-are- skincare-ingredient-to-know-50510.html&psig=AOvVaw3R_C9X_b-

_Nf1jWPv6xyHw&ust=1589381725227000&source=images&cd=vfe&ved=0CAIQjRxqFwoTCPiY6b3KrukCFQAAAAAdAAAA ABAI

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https://www.google.com/url?sa=i&url=https%3A%2F%2Fwww.slideshare.net%2Fprasanthperceptron

%2Fsecondary-structural-elements-ramachandran-

plot&psig=AOvVaw081aKqeekwosuJRpSTpwQs&ust=1589382770169000&source=images&cd=vfe&

ved=0CAIQjRxqFwoTCLjVwLHOrukCFQAAAAAdAAAAABAI

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https://www.google.com/url?sa=i&url=https%3A%2F%2Fdocplayer.biz.tr%2F9005237-Proteinlerin-3-boyutlu-yapisi- bazilari-halat-seklinde-yapisal-islevi-varken-bazilari-kuresel-formda-ve-katalitik-

gorev.html&psig=AOvVaw08j5aTzcS4ZobqDce2OIjr&ust=1589382944878000&source=images&cd=vfe&ved=0CAI QjRxqFwoTCJCYuIbPrukCFQAAAAAdAAAAABAk

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https://www.google.com/url?sa=i&url=https%3A%2F%2Fbiochemianzunited.wordpress.com

%2F2014%2F03%2F04%2F289%2F&psig=AOvVaw2rYZJ2ylXrZr_oKHucO59n&ust=15893821759 80000&source=images&cd=vfe&ved=0CAIQjRxqFwoTCJCAlp3MrukCFQAAAAAdAAAAABBN

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• From these multiple conformation, one or more of these constituents predominantly function under biological conditions.

• Under certain conditions, the existing conformation is

having the thermodynamically most stable free energy

(natural proteins).

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https://www.google.com/url?sa=i&url=http%3A%2F%2Fwww.cryst.bbk.ac.uk

%2FPPS95%2Fcourse%2F3_geometry%2Frama.html&psig=AOvVaw3roP99Lh717FloSJ8Y- bRI&ust=1589381919330000&source=images&cd=vfe&ved=0CAIQjRxqFwoTCNjDrarLrukCFQ AAAAAdAAAAABAI

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REFERENCES

MAIN : Lehninger Principles of Biochemistry, David

L. Nelson, Michael M. Cox, 5th Edition, 2013.

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Principles of Biochemistry, H. R. Horton, L. A.

Moran, K. G. Scrimgeour, M. D. Perry, J. D. Rawn, Pearson Prentis Hall, 2006.

Color Atlas of Biochemistry, J. Koolman, K. H.

Roehm, Georg Thieme Verlag, 2005.

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Harper’s Illustrated BiochemIstry, R. K. Murray, D. K. Granner, P. A. Mayes, V. W. Rodwell, Lange Medical Books/McGraw-Hill Medical PublishIng DIvIsIon, 2003.

Basic Concepts in Biochemistry, A Student’s Survival Guide, H. F. Gilbert, McGraw-Hill Health Proffesions Division, 2000.

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