TY - CHAP
T1 - Introduction to Protein Folding
AU - Gils, Juami H. M. van
AU - Dijk, Erik van
AU - May, Ali
AU - Mouhib, Halima
AU - Bijlard, Jochem
AU - Jacobsen, Annika
AU - Houtkamp, Isabel
AU - Feenstra, K. Anton
AU - Abeln, Sanne
N1 - editorial responsability: Juami H. M. van Gils, K. Anton Feenstra, Sanne Abeln. This chapter is part of the book "Introduction to Protein Structural Bioinformatics". The Preface arXiv:1801.09442 contains links to all the (published) chapters. The update adds available arxiv hyperlinks for the chapters
PY - 2023/7/5
Y1 - 2023/7/5
N2 - While many good textbooks are available on Protein Structure, Molecular Simulations, Thermodynamics and Bioinformatics methods in general, there is no good introductory level book for the field of Structural Bioinformatics. This book aims to give an introduction into Structural Bioinformatics, which is where the previous topics meet to explore three dimensional protein structures through computational analysis. We provide an overview of existing computational techniques, to validate, simulate, predict and analyse protein structures. More importantly, it will aim to provide practical knowledge about how and when to use such techniques. We will consider proteins from three major vantage points: Protein structure quantification, Protein structure prediction, and Protein simulation & dynamics. In this chapter we explore basic physical and chemical concepts required to understand protein folding. We introduce major (de)stabilising factors of folded protein structures such as the hydrophobic effect and backbone entropy. In addition, we consider different states along the folding pathway, as well as natively disordered proteins and aggregated protein states. In this chapter, an intuitive understanding is provided about the protein folding process, to prepare for the next chapter on the thermodynamics of protein folding. In particular, it is emphasized that protein folding is a stochastic process and that proteins unfold and refold in a dynamic equilibrium. The effect of temperature on the stability of the folded and unfolded states is also explained.
AB - While many good textbooks are available on Protein Structure, Molecular Simulations, Thermodynamics and Bioinformatics methods in general, there is no good introductory level book for the field of Structural Bioinformatics. This book aims to give an introduction into Structural Bioinformatics, which is where the previous topics meet to explore three dimensional protein structures through computational analysis. We provide an overview of existing computational techniques, to validate, simulate, predict and analyse protein structures. More importantly, it will aim to provide practical knowledge about how and when to use such techniques. We will consider proteins from three major vantage points: Protein structure quantification, Protein structure prediction, and Protein simulation & dynamics. In this chapter we explore basic physical and chemical concepts required to understand protein folding. We introduce major (de)stabilising factors of folded protein structures such as the hydrophobic effect and backbone entropy. In addition, we consider different states along the folding pathway, as well as natively disordered proteins and aggregated protein states. In this chapter, an intuitive understanding is provided about the protein folding process, to prepare for the next chapter on the thermodynamics of protein folding. In particular, it is emphasized that protein folding is a stochastic process and that proteins unfold and refold in a dynamic equilibrium. The effect of temperature on the stability of the folded and unfolded states is also explained.
KW - q-bio.BM
U2 - 10.48550/arXiv.2307.02174
DO - 10.48550/arXiv.2307.02174
M3 - Chapter
BT - Introduction to Structural Bioinformatics
ER -