TY - CHAP
T1 - Natural constraints, folding, motion, and structural stability in transmembrane helical proteins
AU - Harrington, Susan E.
AU - Ben-Tal, Nir
PY - 2010
Y1 - 2010
N2 - Transmembrane (TM) helical proteins are of fundamental importance in many diverse biological processes. To understand these proteins functionally, it is necessary to characterize the forces that stabilize them. What are these forces (both within the protein itself and between the protein and membrane) and how do they give rise to the multiple conformational states and complex activity of TM helical proteins? How do they act in concert to fold TM helical proteins, create their low-energy stable states, and guide their motion? These central questions have led to the description of critical natural constraints and partial answers, which we will review. We will then describe how these constraints can be tracked through homologs and proteins of similar folds in order to better understand how amino acid sequence can specify structure and guide motion. Our emphasis throughout will be on structural features of TM helix bundles themselves, but we will also sketch the membrane-related aspects of these questions.
AB - Transmembrane (TM) helical proteins are of fundamental importance in many diverse biological processes. To understand these proteins functionally, it is necessary to characterize the forces that stabilize them. What are these forces (both within the protein itself and between the protein and membrane) and how do they give rise to the multiple conformational states and complex activity of TM helical proteins? How do they act in concert to fold TM helical proteins, create their low-energy stable states, and guide their motion? These central questions have led to the description of critical natural constraints and partial answers, which we will review. We will then describe how these constraints can be tracked through homologs and proteins of similar folds in order to better understand how amino acid sequence can specify structure and guide motion. Our emphasis throughout will be on structural features of TM helix bundles themselves, but we will also sketch the membrane-related aspects of these questions.
UR - http://www.scopus.com/inward/record.url?scp=84889819324&partnerID=8YFLogxK
U2 - 10.1007/978-3-7091-0045-5_12
DO - 10.1007/978-3-7091-0045-5_12
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AN - SCOPUS:84889819324
SN - 9783709100448
SP - 205
EP - 229
BT - Structural Bioinformatics of Membrane Proteins
PB - Springer Vienna
ER -