SINGLE PROTON EXCHANGE KINETICS IN PROTEINS
蛋白质中的单质子交换动力学
基本信息
- 批准号:3273761
- 负责人:
- 金额:$ 15.27万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1979
- 资助国家:美国
- 起止时间:1979-04-01 至 1990-03-31
- 项目状态:已结题
- 来源:
- 关键词:acidity /alkalinity bacterial proteins chemical reaction conformation crosslink deuterium globular protein hydrogen transport isomorphous substitution molecular rearrangement nuclear magnetic resonance spectroscopy peptide chemical synthesis protein structure stop flow technique thermodynamics trypsin inhibitors
项目摘要
The general goal of this project is to determine the internal motions of
proteins by which atoms buried in the matrix of folded proteins are
accessible to solvent. This is measured by the hydrogen isotope exchange
kinetics of solvent hydrogen atoms with labile protein protons, most of
which are peptide amide protons. The hydrogen isotope exchange kinetics of
peptide NN's in folded proteins are distributed over 6-10 orders of
magnitude. The most rapidly exchangeing NH's are on the surface, and the
slowest exchanging NH's tend to be in buried sections of Beta -sheet.
Although buried NH's exchange slower than model compounds, their finite
exchange rates demonstrate that interior atoms in native proteins have some
probability of being exposed to solvent. This immediately implies that the
protein fluctuates to render tightly packed, buried atoms accessible to
solvent.
Recently our laboratory has made the exciting findings that the exchange
rates of NH's on the surface of bovine pancreatic trypsin inhibitor (BPTI)
vary from 3-fold to 2000-fold slower than model compounds, that their pHmin
values vary over greater than 2 pH units, and that some have pHmin of less
than 1. It has been commonly assumed that surface NH atoms (not H-bonded
and with finite static accessibility) exchange with rates comparable to
those in model peptides. The deviation in exchange rates and pHmin from
model compounds then taken on special interest as a reflection of the
dynamic structure of the protein-solvent interface.
The specific aims of this research proposal are 1) to characterize the
hydrogen exchange kinetics of NH's in BPTI with intermediate exchange
rates, 2) to measure the effect of trypsinogen and trypsinogen/Ile-Val
binding on the exchange rates of BPTI NH's 3) to compare the exchange rate
of individual BPTI NH's in solution with their exchange rates in the
crystalline and powder forms, and 4) to measure the exchange kinetics of
water buried in the BPTI-trypsin complex with solvent water.
这个项目的总体目标是确定的内部运动
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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{{ truncateString('CLARE K WOODWARD', 18)}}的其他基金
DETERMINATION OF ASP26 PKA IN REDUCED THIOREDOXIN
还原型硫氧还蛋白中 ASP26 PKA 的测定
- 批准号:
6251987 - 财政年份:1997
- 资助金额:
$ 15.27万 - 项目类别:
THIOREDOXIN AND GLUTAREDOXIN STABILITY AND FUNCTION
硫氧还蛋白和谷氧还蛋白的稳定性和功能
- 批准号:
2185682 - 财政年份:1993
- 资助金额:
$ 15.27万 - 项目类别:
THIOREDOXIN AND GLUTAREDOXIN STABILITY AND FUNCTION
硫氧还蛋白和谷氧还蛋白的稳定性和功能
- 批准号:
2185683 - 财政年份:1993
- 资助金额:
$ 15.27万 - 项目类别:
THIOREDOXIN AND GLUTAREDOXIN STABILITY AND FUNCTION
硫氧还蛋白和谷氧还蛋白的稳定性和功能
- 批准号:
3307679 - 财政年份:1993
- 资助金额:
$ 15.27万 - 项目类别:
THIOREDOXIN AND GLUTAREDOXIN STABILITY AND FUNCTION
硫氧还蛋白和谷氧还蛋白的稳定性和功能
- 批准号:
2185684 - 财政年份:1993
- 资助金额:
$ 15.27万 - 项目类别:
1992 BIOPOLYMERS GORDON RESEARCH CONFERENCE
1992 年生物聚合物戈登研究会议
- 批准号:
3435193 - 财政年份:1992
- 资助金额:
$ 15.27万 - 项目类别:
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