PPT-PROTEIN STRUCTURE

PROTEIN STRUCTURE To understand how drugs interact it is necessary to understand their structure Proteins have four level of structure PRIMARY SECONDARY TERTIARY QUATERNARY 1PRIMARY STRUCTURE. Sequence:. Edman degradation. Mass spectrometry. Secondary structure:. Circular Dichroism. FTIR. Tertiary, quaternary structure:. NMR. X-ray crystallography. Protein sequencing approaches depend on what is known and what is the goal. Alexey Onufriev, . Virginia Tech. www.cs.vt.edu/~onufriev. Proteins play key roles in a living system. Three (out of many many) examples of protein functions. Catalysis:. Almost all chemical reactions in a living cell are catalyzed by protein enzymes.. Sequence:. Edman degradation. Mass spectrometry. Secondary structure:. Circular Dichroism. FTIR. Tertiary, quaternary structure:. NMR. X-ray crystallography. Protein sequencing approaches depend on what is known and what is the goal. Proteins account for more than 50% of the dry mass of most cells. Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances. Contains . carbon, hydrogen. , oxygen, and nitrogen. Remember carbohydrates and lipids contain carbon, hydrogen, and oxygen – SO protein adds . nitrogen. Some proteins also contain sulfur, iron. , copper, phosphorus, or . LapA. in LPS Assembly. Aarthi Prakash. December 1, 2017. Lipopolysaccharide. Outer membrane of E. Coli. LPS . 6 Fatty Acyl Side Chains with many sugars attached. LPS bind together. Provides gel like barrier. VBC-603. P.G.. 30.12.2020. Protein . Strucuture. Sequence, Structure and Function. What determines fold?. Anfinsen’s experiments in 1957 demonstrated that proteins can fold spontaneously into their native conformations under physiological conditions. This implies that primary structure does indeed determine folding or 3-D . Program for today:. - . Structures. . from. . p. rotein. X-. ray. . crystallography. - . Statistics. . of. . protein. . structures. - Statistical . potentials. 1. V10. Processing of Biological Data. Dr. . Shaimaa. . Munther. . Learning Outcomes - Proteins. Define the levels of protein conformation and to indicate the role of weak interactions.. Illustrate how protein structure relates to protein function using examples.. Proteins are biopolymers, made of the 20 L- . α. -amino acids linked by peptide bonds.. Polypeptide backbone is a repeating sequence of. . N-C-C-N-C-C…. The side chain or R group is not a part of the backbone or the peptide bond.. Localized arrangement of adjacent amino acids formed as the polypeptide chain folds.. The regions of ordered structures formed by interaction of hydrogen bond donor and hydrogen bond acceptor residues of the repeating peptide unit. Prediction . Wang Yang. 2014.1.3. Outline. Molecular. . Co-evolution . phenomenon. A. pplications . of Co-evolution . in . protein structure prediction and PPI prediction.. Co-evolution measurement: . Virginia Tech. www.cs.vt.edu/~onufriev. Gene is protein. ’. s blueprint, genome is life. ’. s blueprint . Gene. Genome. DNA. Protein. Gene. Gene. Gene. Gene. Gene. Gene. Gene. Gene. Gene. Gene. Gene. This has proved to be a very challenging problem. It has aptly been described as the second half of the genetic code, and as the three-dimensional code, as opposed to the one-dimensional code involved in nucleotide/amino acid sequence. .