Salt Bridges in a-Helices Formed by Short Peptides of de Novo Design

鲍德温博士将继续研究短螺旋肽的稳定力。他先前已经证明短肽能够在水溶液中形成单体螺旋。螺旋稳定性在很大程度上取决于这组肽的残基间距，因此可能通过盐桥实现螺旋稳定。他现在将扩展这项研究，包括其他可能形成盐桥的带电残基对，以评估这些盐桥的螺旋稳定特性，如果它们存在的话，并进一步探讨盐桥和非氢键离子对稳定-螺旋的机理。由新设计的短螺旋形成的盐桥只有少数科学家在研究。设计螺旋的研究与人类蛋白含螺旋片段的天然肽形成-螺旋的研究密切相关。这项工作的广泛意义在于，在折叠过程的早期阶段形成的短螺旋能够在蛋白质折叠途径中发挥指导作用

Dr. Baldwin will continue his investigation of the stabilization forces of short helical peptides. He has previously shown that short peptides are able to form monomeric -helices in aqueous solution. Helical stability depended strongly on residue spacing in this set of peptides and therefore helix stabilization by salt bridges was likely. He will now extend this study to include other pairs of charged residues potentially able to form salt bridges in order to evaluate the helix-stabilizing properties of these salt bridges, if they exist, and to investigate further the mechanism of -helix stabilization by salt bridges and non-H- bonded ion pairs. Salt bridges formed by short helices of de novo design are being studied by only a few scientists. The study of designed helices is closely related to the study of -helix formation by naturally occurring peptides derived from helix- containing segments of peoteins. The broad significance of this work is that short helices, formed at early stages in the folding process, have the ability to play a directing role in the pathway of protein folding.***//